PCDAC_PANTR
ID PCDAC_PANTR Reviewed; 941 AA.
AC Q5DRF2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protocadherin alpha-12;
DE Short=PCDH-alpha-12;
DE Flags: Precursor;
GN Name=PCDHA12;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15744052; DOI=10.1534/genetics.104.037606;
RA Wu Q.;
RT "Comparative genomics and diversifying selection of the clustered
RT vertebrate protocadherin genes.";
RL Genetics 169:2179-2188(2005).
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}.
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DR AlphaFoldDB; Q5DRF2; -.
DR SMR; Q5DRF2; -.
DR InParanoid; Q5DRF2; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF15974; Cadherin_tail; 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; 6.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..941
FT /note="Protocadherin alpha-12"
FT /id="PRO_0000003907"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..941
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..350
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..455
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 581..678
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 734..737
FT /note="PXXP 1"
FT REPEAT 790..793
FT /note="PXXP 2"
FT REPEAT 823..826
FT /note="PXXP 3"
FT REPEAT 863..866
FT /note="PXXP 4"
FT REPEAT 882..885
FT /note="PXXP 5"
FT REGION 734..885
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 818..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 941 AA; 101631 MW; BB0D259F31EB7FED CRC64;
MVIIGPRGPG SQRLLLSLLL LAAWEVGSGQ LHYSVYEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKR HGDLLEVNLQ NGILFVNSRI DREKLCGRSA ECSIHLEVIV DRPLQVFHVD
VEVKDINDNP PVFREREQKV PVSESAPLDS HFPLEGASDA DIGVNSLLTY ALSLNEHFEL
KIKTKKDKSI LPELVLRKLL DREQTPKLNL LLMVIDGGKP ELTGSVQIQI TVLDVNDNGP
AFDKPSYKVV LSENVQNDTR VIQLNASDPD EGLNGEISYG IKMILPVSEK CMFSINPDTG
EIRIYGELDF EENNAYEIQV NAIDKGIPSM AGHSMVLVEV LDVNDNVPEV MVTSLSLPVQ
EDAQVGTVIA LISVSDRDSG ANGQVICSLT PHVPFKLVST YKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATAR VSVEVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAW
DADAQKNALV SYSLVERRVG EHALSSYVSV HAESGKVYAL QPLDHEELEL LQFQVSARDA
GVPPLGSNVT LQVFVLDEND NAPALLATPA GSAGGAVSEL VPRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQPAAVGAHI PFHVGLYTGE ISTTRILDEA DAPRHRLLVL VKDHGEPALT
STATVLVSLV ENGQAPKTSS RASVGAVDPE AALVDINVYL IIAICAVSSL LVLTLLLYTA
LRCSAPPTVS RCAPGKPTLV CSSAVGSWSY SQQRRQRVCS GESPPKTDLM AFSPSLQLSR
EDCLNPPSEP RQPNPDWRYS ASLRAGMHSS VHLEEAGILR AGPGGPDQQW PTVSSATPEP
EAGEVSPPVG AGVNSNSWTF KYGPGNPKQS GPGELPDKFI IPGSPAIISI RQEPANSQID
KSDFITFGKK EETKKKKKKK KGNKTQEKKE KGNSTTDNSD Q
