ID PCDGC_HUMAN Reviewed; 932 AA. AC O60330; O15100; Q6UW70; Q9Y5D7; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Protocadherin gamma-A12; DE Short=PCDH-gamma-A12; DE AltName: Full=Cadherin-21; DE AltName: Full=Fibroblast cadherin-3; DE Flags: Precursor; GN Name=PCDHGA12; Synonyms=CDH21, FIB3, KIAA0588; ORFNames=UNQ371/PRO707; 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 [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RX PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8; RA Wu Q., Maniatis T.; RT "A striking organization of a large family of human neural cadherin-like RT cell adhesion genes."; RL Cell 97:779-790(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-808. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 311-444. RX PubMed=9199196; DOI=10.1006/bbrc.1997.6707; RA Matsuyoshi N., Imamura S.; RT "Multiple cadherins are expressed in human fibroblasts."; RL Biochem. Biophys. Res. Commun. 235:355-358(1997). CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be CC involved in the establishment and maintenance of specific neuronal CC connections in the brain. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60330-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=O60330-2; Sequence=VSP_008682, VSP_008683; CC -!- SEQUENCE CAUTION: CC Sequence=AAQ89305.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAA25514.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF152321; AAD43715.1; -; mRNA. DR EMBL; AF152506; AAD43767.1; -; mRNA. DR EMBL; AB011160; BAA25514.2; ALT_INIT; mRNA. DR EMBL; AY358946; AAQ89305.1; ALT_SEQ; mRNA. DR EMBL; AB000897; BAA21135.1; -; mRNA. DR CCDS; CCDS4260.1; -. [O60330-1] DR CCDS; CCDS75346.1; -. [O60330-2] DR PIR; PC4299; PC4299. DR RefSeq; NP_003726.1; NM_003735.2. [O60330-1] DR RefSeq; NP_115265.1; NM_032094.1. [O60330-2] DR AlphaFoldDB; O60330; -. DR SMR; O60330; -. DR BioGRID; 117494; 9. DR IntAct; O60330; 2. DR STRING; 9606.ENSP00000252085; -. DR GlyCosmos; O60330; 4 sites, 1 glycan. DR GlyGen; O60330; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; O60330; -. DR PhosphoSitePlus; O60330; -. DR BioMuta; PCDHGA12; -. DR EPD; O60330; -. DR jPOST; O60330; -. DR MassIVE; O60330; -. DR MaxQB; O60330; -. DR PaxDb; 9606-ENSP00000252085; -. DR PeptideAtlas; O60330; -. DR ProteomicsDB; 49346; -. [O60330-1] DR ProteomicsDB; 49347; -. [O60330-2] DR Antibodypedia; 57527; 19 antibodies from 6 providers. DR DNASU; 26025; -. DR Ensembl; ENST00000252085.4; ENSP00000252085.3; ENSG00000253159.3. [O60330-1] DR Ensembl; ENST00000613314.1; ENSP00000481438.1; ENSG00000253159.3. [O60330-2] DR GeneID; 26025; -. DR KEGG; hsa:26025; -. DR MANE-Select; ENST00000252085.4; ENSP00000252085.3; NM_003735.3; NP_003726.1. DR UCSC; uc003lkt.3; human. [O60330-1] DR AGR; HGNC:8699; -. DR CTD; 26025; -. DR DisGeNET; 26025; -. DR GeneCards; PCDHGA12; -. DR HGNC; HGNC:8699; PCDHGA12. DR HPA; ENSG00000253159; Tissue enhanced (brain). DR MalaCards; PCDHGA12; -. DR MIM; 603059; gene. DR MIM; 604968; gene. DR neXtProt; NX_O60330; -. DR OpenTargets; ENSG00000253159; -. DR PharmGKB; PA33047; -. DR VEuPathDB; HostDB:ENSG00000253159; -. DR eggNOG; KOG3594; Eukaryota. DR GeneTree; ENSGT00940000164062; -. DR HOGENOM; CLU_006480_3_0_1; -. DR InParanoid; O60330; -. DR OMA; APYFRED; -. DR OrthoDB; 5402790at2759; -. DR PhylomeDB; O60330; -. DR TreeFam; TF332299; -. DR PathwayCommons; O60330; -. DR SignaLink; O60330; -. DR SIGNOR; O60330; -. DR BioGRID-ORCS; 26025; 10 hits in 1094 CRISPR screens. DR GeneWiki; PCDHGA12; -. DR GenomeRNAi; 26025; -. DR Pharos; O60330; Tdark. DR PRO; PR:O60330; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O60330; Protein. DR Bgee; ENSG00000253159; Expressed in stromal cell of endometrium and 97 other cell types or tissues. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro. DR GO; GO:0007399; P:nervous system development; IEA:UniProt. DR CDD; cd11304; Cadherin_repeat; 6. DR Gene3D; 2.60.40.60; Cadherins; 6. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR032455; Cadherin_C. DR InterPro; IPR031904; Cadherin_CBD. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR013164; Cadherin_N. DR PANTHER; PTHR24028; CADHERIN-87A; 1. DR PANTHER; PTHR24028:SF227; PROTOCADHERIN GAMMA-A12; 1. DR Pfam; PF00028; Cadherin; 5. DR Pfam; PF08266; Cadherin_2; 1. DR Pfam; PF16492; Cadherin_C_2; 1. DR Pfam; PF15974; Cadherin_tail; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 6. DR SUPFAM; SSF49313; Cadherin-like; 6. DR PROSITE; PS00232; CADHERIN_1; 5. DR PROSITE; PS50268; CADHERIN_2; 6. DR Genevisible; O60330; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein; KW Membrane; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..932 FT /note="Protocadherin gamma-A12" FT /id="PRO_0000003970" FT TOPO_DOM 30..692 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 693..713 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 714..932 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..133 FT /note="Cadherin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 134..242 FT /note="Cadherin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 243..347 FT /note="Cadherin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 348..452 FT /note="Cadherin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 453..562 FT /note="Cadherin 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 570..683 FT /note="Cadherin 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT REGION 803..841 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..932 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 813..841 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 419 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 545 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 809..820 FT /note="QAPPNTDWRFSQ -> VSLYQIFFLFFF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10380929" FT /id="VSP_008682" FT VAR_SEQ 821..932 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10380929" FT /id="VSP_008683" FT CONFLICT 331 FT /note="A -> P (in Ref. 4; BAA21135)" FT /evidence="ECO:0000305" SQ SEQUENCE 932 AA; 100955 MW; 8BDA90084785D746 CRC64; MIPARLHRDY KGLVLLGILL GTLWETGCTQ IRYSVPEELE KGSRVGDISR DLGLEPRELA ERGVRIIPRG RTQLFALNPR SGSLVTAGRI DREELCMGAI KCQLNLDILM EDKVKIYGVE VEVRDINDNA PYFRESELEI KISENAATEM RFPLPHAWDP DIGKNSLQSY ELSPNTHFSL IVQNGADGSK YPELVLKRAL DREEKAAHHL VLTASDGGDP VRTGTARIRV MVLDANDNAP AFAQPEYRAS VPENLALGTQ LLVVNATDPD EGVNAEVRYS FRYVDDKAAQ VFKLDCNSGT ISTIGELDHE ESGFYQMEVQ AMDNAGYSAR AKVLITVLDV NDNAPEVVLT SLASSVPENS PRGTLIALLN VNDQDSEENG QVICFIQGNL PFKLEKSYGN YYSLVTDIVL DREQVPSYNI TVTATDRGTP PLSTETHISL NVADTNDNPP VFPQASYSAY IPENNPRGVS LVSVTAHDPD CEENAQITYS LAENTIQGAS LSSYVSINSD TGVLYALSSF DYEQFRDLQV KVMARDNGHP PLSSNVSLSL FVLDQNDNAP EILYPALPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL TVAVADSIPQ VLADLGSLES PANSETSDLT LYLVVAVAAV SCVFLAFVIL LLALRLRRWH KSRLLQASGG GLTGAPASHF VGVDGVQAFL QTYSHEVSLT TDSRKSHLIF PQPNYADMLV SQESFEKSEP LLLSGDSVFS KDSHGLIEQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK //