ID CABP2_HUMAN Reviewed; 220 AA. AC Q9NPB3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 4. DT 07-OCT-2020, entry version 152. DE RecName: Full=Calcium-binding protein 2; DE Short=CaBP2; GN Name=CABP2; 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] (ISOFORMS L-CABP2 AND S-CABP2), RP VARIANT GLN-94, AND MYRISTOYLATION AT GLY-2. 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 GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). 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). RN [5] RP INVOLVEMENT IN DFNB93. RX PubMed=22981119; DOI=10.1016/j.ajhg.2012.08.018; RA Schrauwen I., Helfmann S., Inagaki A., Predoehl F., Tabatabaiefar M.A., RA Picher M.M., Sommen M., Seco C.Z., Oostrik J., Kremer H., Dheedene A., RA Claes C., Fransen E., Chaleshtori M.H., Coucke P., Lee A., Moser T., RA Van Camp G.; RT "A mutation in CABP2, expressed in cochlear hair cells, causes autosomal- RT recessive hearing impairment."; RL Am. J. Hum. Genet. 91:636-645(2012). RN [6] RP VARIANT DFNB93 156-GLU--ARG-216 DEL, AND FUNCTION. RX PubMed=28183797; DOI=10.1073/pnas.1617533114; RA Picher M.M., Gehrt A., Meese S., Ivanovic A., Predoehl F., Jung S., RA Schrauwen I., Dragonetti A.G., Colombo R., Van Camp G., Strenzke N., RA Moser T.; RT "Ca(2+)-binding protein 2 inhibits Ca(2+)-channel inactivation in mouse RT inner hair cells."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E1717-E1726(2017). CC -!- FUNCTION: Required for sound encoding at inner hair cells (IHCs) CC synapses, likely via inhibition of the inactivation of voltage-gated CC calcium channel of type 1.3 (Cav1.3) in the IHCs (PubMed:28183797). CC Required for the normal transfer of light signals through the retina CC (By similarity). {ECO:0000250|UniProtKB:Q9JLK4, CC ECO:0000269|PubMed:28183797}. CC -!- INTERACTION: CC Q9NPB3; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-12011224, EBI-7600130; CC Q9NPB3; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-12011224, EBI-17439331; CC Q9NPB3; Q5T686: AVPI1; NbExp=3; IntAct=EBI-12011224, EBI-8640233; CC Q9NPB3; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-12011224, EBI-12155483; CC Q9NPB3; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-12011224, EBI-7317823; CC Q9NPB3; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-12011224, EBI-11530605; CC Q9NPB3; Q5JTJ3: COA6; NbExp=3; IntAct=EBI-12011224, EBI-2874677; CC Q9NPB3; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-12011224, EBI-18398199; CC Q9NPB3; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-12011224, EBI-2349927; CC Q9NPB3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12011224, EBI-5916454; CC Q9NPB3; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-12011224, EBI-10961706; CC Q9NPB3; P35452-2: HOXD12; NbExp=3; IntAct=EBI-12011224, EBI-17244356; CC Q9NPB3; Q9BRK3: MXRA8; NbExp=3; IntAct=EBI-12011224, EBI-11721798; CC Q9NPB3; Q9BU61: NDUFAF3; NbExp=3; IntAct=EBI-12011224, EBI-2114801; CC Q9NPB3; O00746: NME4; NbExp=3; IntAct=EBI-12011224, EBI-744871; CC Q9NPB3; Q9NPE3: NOP10; NbExp=3; IntAct=EBI-12011224, EBI-1642169; CC Q9NPB3; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-12011224, EBI-2949792; CC Q9NPB3; P86480: PRR20D; NbExp=3; IntAct=EBI-12011224, EBI-12754095; CC Q9NPB3; Q7Z3Z2: RD3; NbExp=3; IntAct=EBI-12011224, EBI-10257497; CC Q9NPB3; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-12011224, EBI-10269322; CC Q9NPB3; O43623: SNAI2; NbExp=3; IntAct=EBI-12011224, EBI-9876238; CC Q9NPB3; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-12011224, EBI-11995806; CC Q9NPB3; Q96M29: TEKT5; NbExp=3; IntAct=EBI-12011224, EBI-10239812; CC Q9NPB3; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-12011224, EBI-3925505; CC Q9NPB3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12011224, EBI-11741437; CC Q9NPB3; P19237: TNNI1; NbExp=3; IntAct=EBI-12011224, EBI-746692; CC Q9NPB3; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-12011224, EBI-17716262; CC Q9NPB3; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-12011224, EBI-12817837; CC Q9NPB3; Q8TAG6: VXN; NbExp=3; IntAct=EBI-12011224, EBI-12071548; CC Q9NPB3; P52738: ZNF140; NbExp=3; IntAct=EBI-12011224, EBI-12069140; CC Q9NPB3; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-12011224, EBI-8490788; CC Q9NPB3; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-12011224, EBI-10251462; CC Q9NPB3; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-12011224, EBI-3925400; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:19338761}. Cell membrane CC {ECO:0000269|PubMed:19338761}; Lipid-anchor CC {ECO:0000269|PubMed:19338761}; Cytoplasmic side CC {ECO:0000269|PubMed:19338761}. Golgi apparatus CC {ECO:0000269|PubMed:19338761}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=L-CaBP2; CC IsoId=Q9NPB3-1; Sequence=Displayed; CC Name=S-CaBP2; CC IsoId=Q9NPB3-2; Sequence=VSP_000734; CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:11108966}. CC -!- DISEASE: Deafness, autosomal recessive, 93 (DFNB93) [MIM:614899]: A CC form of non-syndromic deafness characterized by stable, bilateral, CC symmetric, prelingual moderate to severe deafness. Hearing impairment CC is slightly more pronounced in the mid-frequencies, resulting in a CC distinctive shallow U-shaped audiogram. {ECO:0000269|PubMed:22981119, CC ECO:0000269|PubMed:28183797}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF170811; AAF26283.1; -; Genomic_DNA. DR EMBL; AF169154; AAF25788.1; -; mRNA. DR EMBL; AP001184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS8170.1; -. [Q9NPB3-1] DR RefSeq; NP_001305425.1; NM_001318496.1. DR RefSeq; NP_057450.2; NM_016366.2. [Q9NPB3-1] DR SMR; Q9NPB3; -. DR BioGRID; 119560; 43. DR IntAct; Q9NPB3; 33. DR STRING; 9606.ENSP00000294288; -. DR iPTMnet; Q9NPB3; -. DR BioMuta; CABP2; -. DR DMDM; 294862530; -. DR PaxDb; Q9NPB3; -. DR PeptideAtlas; Q9NPB3; -. DR PRIDE; Q9NPB3; -. DR ProteomicsDB; 81957; -. [Q9NPB3-1] DR ProteomicsDB; 81958; -. [Q9NPB3-2] DR Antibodypedia; 67889; 110 antibodies. DR DNASU; 51475; -. DR Ensembl; ENST00000294288; ENSP00000294288; ENSG00000167791. [Q9NPB3-1] DR Ensembl; ENST00000353903; ENSP00000312037; ENSG00000167791. [Q9NPB3-2] DR GeneID; 51475; -. DR KEGG; hsa:51475; -. DR UCSC; uc001omc.2; human. [Q9NPB3-1] DR CTD; 51475; -. DR DisGeNET; 51475; -. DR EuPathDB; HostDB:ENSG00000167791.11; -. DR GeneCards; CABP2; -. DR HGNC; HGNC:1385; CABP2. DR HPA; ENSG00000167791; Tissue enriched (retina). DR MalaCards; CABP2; -. DR MIM; 607314; gene. DR MIM; 614899; phenotype. DR neXtProt; NX_Q9NPB3; -. DR OpenTargets; ENSG00000167791; -. DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB. DR PharmGKB; PA26001; -. DR eggNOG; KOG0027; Eukaryota. DR GeneTree; ENSGT00940000159796; -. DR HOGENOM; CLU_061288_2_2_1; -. DR InParanoid; Q9NPB3; -. DR KO; K23531; -. DR OrthoDB; 1424914at2759; -. DR PhylomeDB; Q9NPB3; -. DR TreeFam; TF334804; -. DR PathwayCommons; Q9NPB3; -. DR BioGRID-ORCS; 51475; 6 hits in 864 CRISPR screens. DR GenomeRNAi; 51475; -. DR Pharos; Q9NPB3; Tbio. DR PRO; PR:Q9NPB3; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9NPB3; protein. DR Bgee; ENSG00000167791; Expressed in testis and 9 other tissues. DR ExpressionAtlas; Q9NPB3; baseline and differential. DR Genevisible; Q9NPB3; HS. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007601; P:visual perception; ISS:UniProtKB. DR CDD; cd00051; EFh; 1. DR InterPro; IPR015754; Ca-bd_2. 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 PANTHER; PTHR45917:SF2; PTHR45917:SF2; 1. DR Pfam; PF00036; EF-hand_1; 1. DR Pfam; PF13499; EF-hand_7; 1. 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 Alternative splicing; Calcium; Cell membrane; Cytoplasm; Deafness; KW Disease mutation; Golgi apparatus; Hearing; Lipoprotein; Membrane; KW Metal-binding; Myristate; Non-syndromic deafness; Polymorphism; KW Reference proteome; Repeat; Sensory transduction; Vision. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..220 FT /note="Calcium-binding protein 2" FT /id="PRO_0000073517" FT DOMAIN 78..113 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 111..146 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 152..187 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 189..220 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CA_BIND 91..102 FT /note="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CA_BIND 165..176 FT /note="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CA_BIND 202..213 FT /note="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:10625670" FT VAR_SEQ 15..71 FT /note="Missing (in isoform S-CaBP2)" FT /evidence="ECO:0000303|PubMed:10625670" FT /id="VSP_000734" FT VARIANT 94 FT /note="R -> Q (in dbSNP:rs2276118)" FT /evidence="ECO:0000269|PubMed:10625670" FT /id="VAR_063087" FT VARIANT 156..216 FT /note="Missing (in DFNB93)" FT /evidence="ECO:0000269|PubMed:28183797" FT /id="VAR_080405" SQ SEQUENCE 220 AA; 24482 MW; 9A0F0E7358A44F3A CRC64; MGNCAKRPWR RGPKDPLQWL GSPPRGSCPS PSSSPKEQGD PAPGVQGYSV LNSLVGPACI FLRPSIAATQ LDRELRPEEI EELQVAFQEF DRDRDGYIGC RELGACMRTL GYMPTEMELI EISQQISGGK VDFEDFVELM GPKLLAETAD MIGVRELRDA FREFDTNGDG RISVGELRAA LKALLGERLS QREVDEILQD VDLNGDGLVD FEEFVRMMSR //