CABP5_HUMAN
ID CABP5_HUMAN Reviewed; 173 AA.
AC Q9NP86; A0AUY4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calcium-binding protein 5;
DE Short=CaBP5;
GN Name=CABP5; Synonyms=CABP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Retina;
RX PubMed=10625670; DOI=10.1074/jbc.275.2.1247;
RA Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H., Tempst P.,
RA Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.;
RT "Five members of a novel Ca(2+)-binding protein (CABP) subfamily with
RT similarity to calmodulin.";
RL J. Biol. Chem. 275:1247-1260(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11108966; DOI=10.1016/s0167-4889(00)00099-9;
RA Sokal I., Li N., Verlinde C.L.M.J., Haeseleer F., Baehr W., Palczewski K.;
RT "Ca(2+)-binding proteins in the retina: from discovery to etiology of human
RT disease.";
RL Biochim. Biophys. Acta 1498:233-251(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=19338761; DOI=10.1016/j.bbrc.2009.01.177;
RA McCue H.V., Burgoyne R.D., Haynes L.P.;
RT "Membrane targeting of the EF-hand containing calcium-sensing proteins
RT CaBP7 and CaBP8.";
RL Biochem. Biophys. Res. Commun. 380:825-831(2009).
CC -!- FUNCTION: Inhibits calcium-dependent inactivation of L-type calcium
CC channel and shifts voltage dependence of activation to more depolarized
CC membrane potentials (By similarity). Involved in the transmission of
CC light signals (By similarity). May positively regulate neurotransmitter
CC vesicle endocytosis and exocytosis in a salt-dependent manner (By
CC similarity). May play a role in the extension and network organization
CC of neurites (By similarity). {ECO:0000250|UniProtKB:Q9JLK3}.
CC -!- SUBUNIT: Interacts with CACNA1C (via C-terminal CDB motif) in a
CC calcium-dependent manner (By similarity). Interacts with STXBP1 (By
CC similarity). Interacts with MYO6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JLK3, ECO:0000250|UniProtKB:Q9N1Q8}.
CC -!- INTERACTION:
CC Q9NP86; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-10311131, EBI-17721098;
CC Q9NP86; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-10311131, EBI-14493093;
CC Q9NP86; A2RRN7: CADPS; NbExp=3; IntAct=EBI-10311131, EBI-10179719;
CC Q9NP86; Q8TAP6: CEP76; NbExp=8; IntAct=EBI-10311131, EBI-742887;
CC Q9NP86; Q8WUE5: CT55; NbExp=3; IntAct=EBI-10311131, EBI-6873363;
CC Q9NP86; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10311131, EBI-742054;
CC Q9NP86; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-10311131, EBI-747204;
CC Q9NP86; Q0VD86: INCA1; NbExp=10; IntAct=EBI-10311131, EBI-6509505;
CC Q9NP86; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10311131, EBI-739832;
CC Q9NP86; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10311131, EBI-741037;
CC Q9NP86; A8MW99: MEI4; NbExp=3; IntAct=EBI-10311131, EBI-19944212;
CC Q9NP86; O00746: NME4; NbExp=3; IntAct=EBI-10311131, EBI-744871;
CC Q9NP86; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-10311131, EBI-10240813;
CC Q9NP86; P25786: PSMA1; NbExp=3; IntAct=EBI-10311131, EBI-359352;
CC Q9NP86; Q04864: REL; NbExp=3; IntAct=EBI-10311131, EBI-307352;
CC Q9NP86; O00560: SDCBP; NbExp=3; IntAct=EBI-10311131, EBI-727004;
CC Q9NP86; P15884: TCF4; NbExp=5; IntAct=EBI-10311131, EBI-533224;
CC Q9NP86; Q08117-2: TLE5; NbExp=5; IntAct=EBI-10311131, EBI-11741437;
CC Q9NP86; P19237: TNNI1; NbExp=3; IntAct=EBI-10311131, EBI-746692;
CC Q9NP86; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-10311131, EBI-2799833;
CC Q9NP86; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-10311131, EBI-12287587;
CC Q9NP86; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-10311131, EBI-14104088;
CC Q9NP86; Q969J2: ZKSCAN4; NbExp=7; IntAct=EBI-10311131, EBI-2818641;
CC Q9NP86; Q14929: ZNF169; NbExp=3; IntAct=EBI-10311131, EBI-10234472;
CC Q9NP86; Q9UK11: ZNF223; NbExp=3; IntAct=EBI-10311131, EBI-10322867;
CC Q9NP86; Q9UJW7: ZNF229; NbExp=3; IntAct=EBI-10311131, EBI-12068564;
CC Q9NP86; P59817: ZNF280A; NbExp=3; IntAct=EBI-10311131, EBI-8489342;
CC Q9NP86; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-10311131, EBI-8643207;
CC Q9NP86; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-10311131, EBI-17269964;
CC Q9NP86; Q9BR84: ZNF559; NbExp=3; IntAct=EBI-10311131, EBI-746605;
CC Q9NP86; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10311131, EBI-4395669;
CC Q9NP86; Q8N3J9: ZNF664; NbExp=3; IntAct=EBI-10311131, EBI-2799450;
CC Q9NP86; Q96BR6: ZNF669; NbExp=3; IntAct=EBI-10311131, EBI-12006574;
CC Q9NP86; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-10311131, EBI-5667516;
CC Q9NP86; Q08AG5: ZNF844; NbExp=3; IntAct=EBI-10311131, EBI-10225757;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19338761}.
CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:11108966}.
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DR EMBL; AF170815; AAF25798.1; -; Genomic_DNA.
DR EMBL; AF170812; AAF25798.1; JOINED; Genomic_DNA.
DR EMBL; AF170813; AAF25798.1; JOINED; Genomic_DNA.
DR EMBL; AF170814; AAF25798.1; JOINED; Genomic_DNA.
DR EMBL; AF169159; AAF25793.1; -; mRNA.
DR EMBL; BC126133; AAI26134.1; -; mRNA.
DR EMBL; BC126135; AAI26136.1; -; mRNA.
DR CCDS; CCDS12709.1; -.
DR RefSeq; NP_062829.1; NM_019855.4.
DR AlphaFoldDB; Q9NP86; -.
DR SMR; Q9NP86; -.
DR BioGRID; 121142; 37.
DR IntAct; Q9NP86; 35.
DR STRING; 9606.ENSP00000293255; -.
DR PhosphoSitePlus; Q9NP86; -.
DR BioMuta; CABP5; -.
DR DMDM; 13431356; -.
DR MassIVE; Q9NP86; -.
DR PaxDb; Q9NP86; -.
DR PeptideAtlas; Q9NP86; -.
DR PRIDE; Q9NP86; -.
DR ProteomicsDB; 81931; -.
DR Antibodypedia; 49583; 192 antibodies from 23 providers.
DR DNASU; 56344; -.
DR Ensembl; ENST00000293255.3; ENSP00000293255.1; ENSG00000105507.3.
DR GeneID; 56344; -.
DR KEGG; hsa:56344; -.
DR MANE-Select; ENST00000293255.3; ENSP00000293255.1; NM_019855.5; NP_062829.1.
DR UCSC; uc002phu.3; human.
DR CTD; 56344; -.
DR DisGeNET; 56344; -.
DR GeneCards; CABP5; -.
DR HGNC; HGNC:13714; CABP5.
DR HPA; ENSG00000105507; Tissue enriched (retina).
DR MIM; 607315; gene.
DR neXtProt; NX_Q9NP86; -.
DR OpenTargets; ENSG00000105507; -.
DR PharmGKB; PA26004; -.
DR VEuPathDB; HostDB:ENSG00000105507; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000160506; -.
DR HOGENOM; CLU_061288_2_2_1; -.
DR InParanoid; Q9NP86; -.
DR OMA; QQVRMNL; -.
DR OrthoDB; 1470794at2759; -.
DR PhylomeDB; Q9NP86; -.
DR TreeFam; TF334804; -.
DR PathwayCommons; Q9NP86; -.
DR SignaLink; Q9NP86; -.
DR BioGRID-ORCS; 56344; 9 hits in 1064 CRISPR screens.
DR GenomeRNAi; 56344; -.
DR Pharos; Q9NP86; Tbio.
DR PRO; PR:Q9NP86; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NP86; protein.
DR Bgee; ENSG00000105507; Expressed in monocyte and 30 other tissues.
DR Genevisible; Q9NP86; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR043582; CaBP1/2/4/5.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45917; PTHR45917; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..173
FT /note="Calcium-binding protein 5"
FT /id="PRO_0000073524"
FT DOMAIN 28..63
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 82..99
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 105..140
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 142..173
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 65
FT /note="T -> R (in dbSNP:rs34862923)"
FT /id="VAR_033695"
FT VARIANT 80
FT /note="L -> P (in dbSNP:rs8105198)"
FT /id="VAR_048633"
FT VARIANT 128
FT /note="V -> A (in dbSNP:rs3745746)"
FT /id="VAR_020020"
FT VARIANT 140
FT /note="E -> K (in dbSNP:rs34681062)"
FT /id="VAR_048634"
FT VARIANT 147
FT /note="I -> S (in dbSNP:rs10425606)"
FT /id="VAR_048635"
SQ SEQUENCE 173 AA; 19826 MW; BB4DD28E9ECC55AF CRC64;
MQFPMGPACI FLRKGIAEKQ RERPLGQDEI EELREAFLEF DKDRDGFISC KDLGNLMRTM
GYMPTEMELI ELGQQIRMNL GGRVDFDDFV ELMTPKLLAE TAGMIGVQEM RDAFKEFDTN
GDGEITLVEL QQAMQRLLGE RLTPREISEV VREADVNGDG TVDFEEFVKM MSR
