PCDAD_PANTR
ID PCDAD_PANTR Reviewed; 950 AA.
AC Q5DRF1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protocadherin alpha-13;
DE Short=PCDH-alpha-13;
DE Flags: Precursor;
GN Name=PCDHA13;
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; Q5DRF1; -.
DR SMR; Q5DRF1; -.
DR InParanoid; Q5DRF1; -.
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..950
FT /note="Protocadherin alpha-13"
FT /id="PRO_0000003909"
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..950
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..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 774..777
FT /note="PXXP 2"
FT REPEAT 799..802
FT /note="PXXP 3"
FT REPEAT 832..835
FT /note="PXXP 4"
FT REPEAT 873..876
FT /note="PXXP 5"
FT REPEAT 891..894
FT /note="PXXP 6"
FT REGION 734..894
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 774..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
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 950 AA; 102228 MW; A3E95D377EE9E1BC CRC64;
MLSSWQGGPR PRQLLLWLLI LAAWETGSGQ LHYSVPEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKT HGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSVHLEVIV DRPLQVFHVE
VKVRDINDNP PIFPESKKRI IVAESRPPET RFPLDGASDA DIGVNSALTY RLDPNDYFTL
DAQNSLEQMS SLSLVLRKTL DREEIQEHSL LLTASDGGKP ELTGTVQLLI TILDVNDNAP
EFYQSVYKVT VLENAFNGTL VIKLNATDPD DGTNGDIVYS FRRPVSPAVV YAFTINPNNG
EIRTKGKLDF EEKKLYEISV EAVDKGNIPM AGHCTLLVEV LDVNDNAPEV TITSLSLPIR
EDTQPSAIIA LISVSDRDSG SNGQVTCTLT PHVPFKLVST YKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATAS VSVGVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAQ
DADAQENALV SYSLVERRVG ERALSSYVSV HAESGKVYAL QPLDHEELEL LQFQVSARDS
GVPPLGSNVT LQVFVLDEND NAPALLTPGA GSAGGTVSEL MPRSVGAGHV VVKVRAVDAD
SGYNAWLSYE LQLAAVGARI PFCVGLYTGE ISTTRPLDEV DAPHHRLLVL VKDHGEPALT
ATATVLLSLV ESGQAPQASS RASAGAVGPE AALVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSAPPTEG VCAPGKPTLV CSSAAGSWSY SQQRRPRVCS GEGPHKTDLM AFSPSLPPCL
GSAEGTGQRE EDSEGLKEPR QPNPDWRYSA SLRAGMHSSV HLEEAGILRA GPGGPDQQWP
TVSSATPEPE AGEVSPPVGA GVNSNSWTFK YGPGNPKQSG PGELPDKFII PGSPAIISIR
QEPANSQIDK SDFITFGKKE ETKKKKKKKK GNKTQEKKEK GNSTTDNSDQ
