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Conserved domains on  [gi|71274156|ref|NP_001025052|]
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calcium and integrin-binding family member 4 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12144783)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
101-168 4.28e-11

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274156   101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLNSDDMSEDLLMDLtnhvLSESDLDNDNMLSFSEFEHAM 168
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLELY 66
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
101-168 4.28e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274156   101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLNSDDMSEDLLMDLtnhvLSESDLDNDNMLSFSEFEHAM 168
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 101-169 5.89e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 50.24  E-value: 5.89e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71274156 101 KIEYAFRIYDFNENGFIDEEDLQRIIlrllnsDDMSEDLLMDLTNHVLSESDLDNDNMLSFSEFEHAMA 169
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAAL------KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 57-172 9.79e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274156   57 SLPALRVNPFRDRICRVFSH-----KGMFSFEDVLGMASVFSEQACPSLKIEYAFRIYDFNENGFIDEEDLQRIilrlln 131
Cdd:PTZ00183  42 AMRSLGFEPKKEEIKQMIADvdkdgSGKIDFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRV------ 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71274156  132 SDDMSEDLLMDLTNHVLSESDLDNDNMLSFSEFEHAMAKSP 172
Cdd:PTZ00183 116 AKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
101-173 1.03e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.03e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71274156 101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLnsddmsedllmdltNHVLSESDLDNDNMLSFSEFEHAMAKSPD 173
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW--------------ATLFSEADTDGDGRISREEFVAGMESLFE 64
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
101-168 4.28e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274156   101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLNSDDMSEDLLMDLtnhvLSESDLDNDNMLSFSEFEHAM 168
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 101-169 5.89e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 50.24  E-value: 5.89e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71274156 101 KIEYAFRIYDFNENGFIDEEDLQRIIlrllnsDDMSEDLLMDLTNHVLSESDLDNDNMLSFSEFEHAMA 169
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAAL------KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 57-172 9.79e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274156   57 SLPALRVNPFRDRICRVFSH-----KGMFSFEDVLGMASVFSEQACPSLKIEYAFRIYDFNENGFIDEEDLQRIilrlln 131
Cdd:PTZ00183  42 AMRSLGFEPKKEEIKQMIADvdkdgSGKIDFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRV------ 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71274156  132 SDDMSEDLLMDLTNHVLSESDLDNDNMLSFSEFEHAMAKSP 172
Cdd:PTZ00183 116 AKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
101-173 1.03e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.03e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71274156 101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLnsddmsedllmdltNHVLSESDLDNDNMLSFSEFEHAMAKSPD 173
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW--------------ATLFSEADTDGDGRISREEFVAGMESLFE 64
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 106-179 5.62e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 39.26  E-value: 5.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71274156 106 FRIYDFNENGFIDEEDLQRIILRL---LNSDDMSEDLLMDLTNHVLSESDLDNDNMLSFSEFEHAMAKSPDFMNSFR 179
Cdd:cd15902   5 WMHFDADGNGYIEGKELDSFLRELlkaLNGKDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILPTEENFLLLFR 81
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
101-173 5.68e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71274156 101 KIEYAFRIYDFNENGFIDEEDLQRIILRLLNSDDMSEDLLmdltnhvlSESDLDNDNMLSFSEFEHAMAK--SPD 173
Cdd:COG5126  70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELF--------ARLDTDGDGKISFEEFVAAVRDyyTPD 136
EF-hand_8 pfam13833
EF-hand domain pair;
113-164 1.08e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71274156   113 ENGFIDEEDLQRIiLRLLNSDDMSEDLLmdltNHVLSESDLDNDNMLSFSEF 164
Cdd:pfam13833   1 EKGVITREELKRA-LALLGLKDLSEDEV----DILFREFDTDGDGYISFDEF 47
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 74-164 2.91e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 35.59  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274156  74 FSHKGMFSFEDVLGMASVFSEQACpslKIEYAFRIYDFNENGFIDEEDLQrIILRLLNSDdmSEDLLMDLTNHVLSESDL 153
Cdd:cd16251  11 FRAHGSFNYKKFFEHVGLKQKSED---QIKKVFQILDKDKSGFIEEEELK-YILKGFSIA--GRDLTDEETKALLAAGDT 84

                        90
                ....*....|.
gi 71274156 154 DNDNMLSFSEF 164
Cdd:cd16251  85 DGDGKIGVEEF 95
EF-hand_6 pfam13405
EF-hand domain;
101-126 5.42e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.30  E-value: 5.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 71274156   101 KIEYAFRIYDFNENGFIDEEDLQRII 126
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKAL 26
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 74-170 8.41e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 34.41  E-value: 8.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274156  74 FSHKGMFsfeDVLGMASVFSEQacpslkIEYAFRIYDFNENGFIDEEDLQrIILRLLNSDdmSEDLLMDLTNHVLSESDL 153
Cdd:cd16254  17 FDYKKFF---EMVGLKKKSADD------VKKVFHILDKDKSGFIEEDELK-FVLKGFSPD--GRDLSDKETKALLAAGDK 84

                        90
                ....*....|....*..
gi 71274156 154 DNDNMLSFSEFEHAMAK 170
Cdd:cd16254  85 DGDGKIGIDEFATLVAE 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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