PC11Y_HUMAN
ID PC11Y_HUMAN Reviewed; 1340 AA.
AC Q9BZA8; Q70LR6; Q70LR8; Q70LS0; Q70LS1; Q70LS2; Q70LS3; Q70LS4; Q70LS5;
AC Q8WY34; Q9BZA9; Q9H4E1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protocadherin-11 Y-linked;
DE Short=Protocadherin-11;
DE AltName: Full=Protocadherin on the Y chromosome;
DE Short=PCDH-Y;
DE AltName: Full=Protocadherin prostate cancer;
DE Short=Protocadherin-PC;
DE AltName: Full=Protocadherin-22;
DE Flags: Precursor;
GN Name=PCDH11Y; Synonyms=PCDH11, PCDH22, PCDHY;
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] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11003707; DOI=10.1007/s003350010177;
RA Blanco P., Sargent C.A., Boucher C., Mitchell M., Affara N.;
RT "Conservation of PCDHX in mammals; expression of human X/Y genes
RT predominantly in brain.";
RL Mamm. Genome 11:906-914(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH CTNNB1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Prostatic carcinoma;
RX PubMed=12420223; DOI=10.1038/sj.onc.1205991;
RA Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R.,
RA Friedman R.A., Burchardt M., Chopin D.K., Buttyan R.;
RT "The emergence of protocadherin-PC expression during the acquisition of
RT apoptosis-resistance by prostate cancer cells.";
RL Oncogene 21:7861-7871(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PHE-917 AND
RP LYS-1012.
RC TISSUE=Brain;
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1109 AND 1119-1340, NUCLEOTIDE SEQUENCE
RP [MRNA] OF 213-1340 (ISOFORM 4), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=14727141; DOI=10.1007/s00335-003-3028-7;
RA Blanco-Arias P., Sargent C.A., Affara N.A.;
RT "Protocadherin X (PCDHX) and Y (PCDHY) genes; multiple mRNA isoforms
RT encoding variant signal peptides and cytoplasmic domains.";
RL Mamm. Genome 15:41-52(2004).
RN [5]
RP CHROMOSOMAL TRANSLOCATION WITH ROBO2.
RX PubMed=17357069; DOI=10.1086/512735;
RA Lu W., van Eerde A.M., Fan X., Quintero-Rivera F., Kulkarni S.,
RA Ferguson H., Kim H.-G., Fan Y., Xi Q., Li Q.-G., Sanlaville D., Andrews W.,
RA Sundaresan V., Bi W., Yan J., Giltay J.C., Wijmenga C., de Jong T.P.V.M.,
RA Feather S.A., Woolf A.S., Rao Y., Lupski J.R., Eccles M.R., Quade B.J.,
RA Gusella J.F., Morton C.C., Maas R.L.;
RT "Disruption of ROBO2 is associated with urinary tract anomalies and confers
RT risk of vesicoureteral reflux.";
RL Am. J. Hum. Genet. 80:616-632(2007).
RN [6]
RP VARIANTS PHE-917 AND LYS-1012, AND TISSUE SPECIFICITY.
RX PubMed=16331680; DOI=10.1002/ajmg.b.30229;
RA Durand C.M., Kappeler C., Betancur C., Delorme R., Quach H.,
RA Goubran-Botros H., Melke J., Nygren G., Chabane N., Bellivier F., Szoke A.,
RA Schurhoff F., Rastam M., Anckarsaeter H., Gillberg C., Leboyer M.,
RA Bourgeron T.;
RT "Expression and genetic variability of PCDH11Y, a gene specific to Homo
RT sapiens and candidate for susceptibility to psychiatric disorders.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 141:67-70(2006).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:12420223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9BZA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZA8-2; Sequence=VSP_017998, VSP_017999;
CC Name=3;
CC IsoId=Q9BZA8-3; Sequence=VSP_017996, VSP_017998, VSP_017999;
CC Name=4;
CC IsoId=Q9BZA8-4; Sequence=VSP_017997, VSP_018000;
CC -!- TISSUE SPECIFICITY: Expressed strongly in fetal brain and brain
CC (cortex, amygdala, thalamus, substantia nigra, hippocampus, caudate
CC nucleus and corpus callosum). Expressed at low level in testis.
CC Expressed in apoptosis-resistant cells. {ECO:0000269|PubMed:11003707,
CC ECO:0000269|PubMed:12420223, ECO:0000269|PubMed:14727141,
CC ECO:0000269|PubMed:16331680}.
CC -!- DISEASE: Note=A chromosomal aberration involving PCDH11Y is a cause of
CC multiple congenital abnormalities, including severe bilateral
CC vesicoureteral reflux (VUR) with ureterovesical junction defects.
CC Translocation t(Y;3)(p11;p12) with ROBO2.
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DR EMBL; AJ276803; CAC13122.1; -; mRNA.
DR EMBL; AF277053; AAL55729.1; -; mRNA.
DR EMBL; AF332216; AAK13468.1; -; mRNA.
DR EMBL; AF332217; AAK13469.1; -; mRNA.
DR EMBL; AJ564958; CAD92429.1; -; mRNA.
DR EMBL; AJ564959; CAD92430.1; -; mRNA.
DR EMBL; AJ564960; CAD92431.1; -; mRNA.
DR EMBL; AJ564961; CAD92432.1; -; mRNA.
DR EMBL; AJ564962; CAD92433.1; -; mRNA.
DR EMBL; AJ564963; CAD92434.1; -; mRNA.
DR EMBL; AJ564966; CAD92437.1; -; mRNA.
DR EMBL; AJ564969; CAD92440.1; -; mRNA.
DR CCDS; CCDS14776.1; -. [Q9BZA8-3]
DR CCDS; CCDS14777.1; -. [Q9BZA8-2]
DR CCDS; CCDS76066.1; -. [Q9BZA8-1]
DR RefSeq; NP_001265548.1; NM_001278619.1. [Q9BZA8-3]
DR RefSeq; NP_116753.1; NM_032971.2. [Q9BZA8-3]
DR RefSeq; NP_116754.1; NM_032972.2. [Q9BZA8-2]
DR RefSeq; NP_116755.1; NM_032973.2. [Q9BZA8-1]
DR RefSeq; XP_016885571.1; XM_017030082.1. [Q9BZA8-3]
DR AlphaFoldDB; Q9BZA8; -.
DR SMR; Q9BZA8; -.
DR BioGRID; 123635; 3.
DR IntAct; Q9BZA8; 2.
DR GlyGen; Q9BZA8; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZA8; -.
DR PhosphoSitePlus; Q9BZA8; -.
DR BioMuta; PCDH11Y; -.
DR DMDM; 74762719; -.
DR EPD; Q9BZA8; -.
DR jPOST; Q9BZA8; -.
DR MassIVE; Q9BZA8; -.
DR PeptideAtlas; Q9BZA8; -.
DR PRIDE; Q9BZA8; -.
DR ProteomicsDB; 79796; -. [Q9BZA8-1]
DR ProteomicsDB; 79797; -. [Q9BZA8-2]
DR ProteomicsDB; 79798; -. [Q9BZA8-3]
DR ProteomicsDB; 79799; -. [Q9BZA8-4]
DR Antibodypedia; 596; 91 antibodies from 26 providers.
DR DNASU; 83259; -.
DR Ensembl; ENST00000215473.7; ENSP00000215473.7; ENSG00000099715.14. [Q9BZA8-4]
DR Ensembl; ENST00000333703.8; ENSP00000330552.4; ENSG00000099715.14. [Q9BZA8-3]
DR Ensembl; ENST00000362095.9; ENSP00000355419.5; ENSG00000099715.14. [Q9BZA8-2]
DR Ensembl; ENST00000400457.3; ENSP00000383306.3; ENSG00000099715.14. [Q9BZA8-1]
DR Ensembl; ENST00000622698.4; ENSP00000482115.1; ENSG00000099715.14. [Q9BZA8-3]
DR GeneID; 83259; -.
DR KEGG; hsa:83259; -.
DR UCSC; uc004fql.3; human. [Q9BZA8-1]
DR CTD; 83259; -.
DR DisGeNET; 83259; -.
DR GeneCards; PCDH11Y; -.
DR HGNC; HGNC:15813; PCDH11Y.
DR HPA; ENSG00000099715; Tissue enriched (brain).
DR MIM; 400022; gene.
DR neXtProt; NX_Q9BZA8; -.
DR OpenTargets; ENSG00000099715; -.
DR PharmGKB; PA32997; -.
DR VEuPathDB; HostDB:ENSG00000099715; -.
DR GeneTree; ENSGT00940000158335; -.
DR HOGENOM; CLU_006480_5_2_1; -.
DR InParanoid; Q9BZA8; -.
DR OMA; DSPIMET; -.
DR PhylomeDB; Q9BZA8; -.
DR TreeFam; TF320624; -.
DR PathwayCommons; Q9BZA8; -.
DR SignaLink; Q9BZA8; -.
DR BioGRID-ORCS; 83259; 13 hits in 625 CRISPR screens.
DR ChiTaRS; PCDH11Y; human.
DR GenomeRNAi; 83259; -.
DR Pharos; Q9BZA8; Tbio.
DR PRO; PR:Q9BZA8; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; Q9BZA8; protein.
DR Bgee; ENSG00000099715; Expressed in corpus callosum and 88 other tissues.
DR ExpressionAtlas; Q9BZA8; baseline and differential.
DR Genevisible; Q9BZA8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0061827; C:sperm head; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
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:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Chromosomal rearrangement; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1340
FT /note="Protocadherin-11 Y-linked"
FT /id="PRO_0000232764"
FT TOPO_DOM 29..844
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..1340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..171
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 172..281
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 282..387
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 394..498
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 499..602
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 603..705
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 709..827
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1052..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..21
FT /note="MFRVGFLIISSSSSLSPLLLV -> MTVGFNSDIS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11003707,
FT ECO:0000303|PubMed:12420223"
FT /id="VSP_017996"
FT VAR_SEQ 1044..1053
FT /note="SQRRVTFHLP -> VGIQVSNTTF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14727141"
FT /id="VSP_017997"
FT VAR_SEQ 1044..1048
FT /note="SQRRV -> TDSRT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11003707,
FT ECO:0000303|PubMed:12420223, ECO:0000303|PubMed:12815422"
FT /id="VSP_017998"
FT VAR_SEQ 1049..1340
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11003707,
FT ECO:0000303|PubMed:12420223, ECO:0000303|PubMed:12815422"
FT /id="VSP_017999"
FT VAR_SEQ 1054..1340
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14727141"
FT /id="VSP_018000"
FT VARIANT 917
FT /note="V -> F (in dbSNP:rs2524543)"
FT /evidence="ECO:0000269|PubMed:12815422,
FT ECO:0000269|PubMed:16331680"
FT /id="VAR_026020"
FT VARIANT 1012
FT /note="N -> K (in dbSNP:rs2563389)"
FT /evidence="ECO:0000269|PubMed:12815422,
FT ECO:0000269|PubMed:16331680"
FT /id="VAR_026021"
FT VARIANT 1320
FT /note="A -> T (in dbSNP:rs2556900)"
FT /id="VAR_048576"
SQ SEQUENCE 1340 AA; 146775 MW; 10C1A56510FF4014 CRC64;
MFRVGFLIIS SSSSLSPLLL VSVVRVNTTN CHKCLLSGTY IFAVLLVCVV FHSGAQEKNY
TIREEIPENV LIGNLLKDLN LSLIPNKSLT TTMQFKLVYK TGDVPLIRIE EDTGEIFTTG
ARIDREKLCA GIPRDEHCFY EVEVAILPDE IFRLVKIRFL IEDINDNAPL FPATVINISI
PENSAINSKY TLPAAVDPDV GINGVQNYEL IKSQNIFGLD VIETPEGDKM PQLIVQKELD
REEKDTYVMK VKVEDGGFPQ RSSTAILQVS VTDTNDNHPV FKETEIEVSI PENAPVGTSV
TQLHATDADI GENAKIHFSF SNLVSNIARR LFHLNATTGL ITIKEPLDRE ETPNHKLLVL
ASDGGLMPAR AMVLVNVTDV NDNVPSIDIR YIVNPVNDTV VLSENIPLNT KIALITVTDK
DADHNGRVTC FTDHEIPFRL RPVFSNQFLL ENAAYLDYES TKEYAIKLLA ADAGKPPLNQ
SAMLFIKVKD ENDNAPVFTQ SFVTVSIPEN NSPGIQLMKV SATDADSGPN AEINYLLGPD
APPEFSLDRR TGMLTVVKKL DREKEDKYLF TILAKDNGVP PLTSNVTVFV SIIDQNDNSP
VFTHNEYKFY VPENLPRHGT VGLITVTDPD YGDNSAVTLS ILDENDDFTI DSQTGVIRPN
ISFDREKQES YTFYVKAEDG GRVSRSSSAK VTINVVDVND NKPVFIVPPY NYSYELVLPS
TNPGTVVFQV IAVDNDTGMN AEVRYSIVGG NTRDLFAIDQ ETGNITLMEK CDVTDLGLHR
VLVKANDLGQ PDSLFSVVIV NLFVNESVTN ATLINELVRK SIEAPVTPNT EIADVSSPTS
DYVKILVAAV AGTITVVVVI FITAVVRCRQ APHLKAAQKN MQNSEWATPN PENRQMIMMK
KKKKKKKHSP KNLLLNVVTI EETKADDVDS DGNRVTLDLP IDLEEQTMGK YNWVTTPTTF
KPDSPDLARH YKSASPQPAF QIQPETPLNL KHHIIQELPL DNTFVACDSI SNCSSSSSDP
YSVSDCGYPV TTFEVPVSVH TRPSQRRVTF HLPEGSQESS SDGGLGDHDA GSLTSTSHGL
PLGYPQEEYF DRATPSNRTE GDGNSDPEST FIPGLKKEIT VQPTVEEASD NCTQECLIYG
HSDACWMPAS LDHSSSSQAQ ASALCHSPPL SQASTQHHSP PVTQTIVLCH SPPVTQTIAL
CHSPPPIQVS ALHHSPPLVQ GTALHHSPPS AQASALCYSP PLAQAAAISH SSSLPQVIAL
HRSQAQSSVS LQQGWVQGAN GLCSVDQGVQ GSATSQFYTM SERLHPSDDS IKVIPLTTFA
PRQQARPSRG DSPIMETHPL
