PCDC2_PANTR
ID PCDC2_PANTR Reviewed; 1007 AA.
AC Q5DRE1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protocadherin alpha-C2;
DE Short=PCDH-alpha-C2;
DE Flags: Precursor;
GN Name=PCDHAC2;
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; Q5DRE1; -.
DR SMR; Q5DRE1; -.
DR STRING; 9598.ENSPTRP00000029626; -.
DR PaxDb; Q5DRE1; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5DRE1; -.
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:InterPro.
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 InterPro; IPR030726; PCDHAC2.
DR PANTHER; PTHR24028:SF119; PTHR24028:SF119; 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; 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..42
FT /evidence="ECO:0000255"
FT CHAIN 43..1007
FT /note="Protocadherin alpha-C2"
FT /id="PRO_0000003913"
FT TOPO_DOM 43..708
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..1007
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..148
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 149..257
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 258..365
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 374..469
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 470..579
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 594..691
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 856..859
FT /note="PXXP 1"
FT REPEAT 889..892
FT /note="PXXP 2"
FT REPEAT 930..933
FT /note="PXXP 3"
FT REPEAT 948..951
FT /note="PXXP 4"
FT REGION 856..951
FT /note="4 X 4 AA repeats of P-X-X-P"
FT REGION 885..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1007 AA; 109349 MW; 4A3E88813E0FC1DE CRC64;
MEQAGTRPAA TEHPRLRRPM PWLLLLPLLL LLLLLLPGPA ASQLRYSVPE EQAPGALVGN
VARALGLELR RLGPGCLRIN HLGAPSPRYL ELDLTSGALF VNERIDREAL CEQRPRCLLS
LEVLAHNPVA VSAVEVEILD INDNSPRFPR PNYQLQVSES VAPGARFHIE SAQDPDVGAN
SVQTYELSPS EHFELDLKPL QENSKVLELV LRKGLDREQA ALHHLVLTAV DGGIPARSGT
AQISVRVLDT NDNSPAFDQS TYRVQLREDS PPGTLVVKLN ASDPDEGSNG ELRYSLSSYT
SDRERQLFSI DASTGEVRVI GGLDYEEASS YQIYVQATDR GPVPMAGHCK VLVDIVDVND
NAPEVVLTDL YSPVPENATP NTIVAVLSVN DQDSGPNRKV SLGLEATLPF RLNGFGNSYT
LVVSGPLDRE RVAVYNITVT ATDGGIPQLT SLRTLKVEIS DINDNPPSFL EDSYSIYIQE
NNLPGVLLCT VQATDPDEKE NAEVTYSLLE REIQGLPVTS YVSINSASGS LYAVNSFDYE
KFREFFVTVE AQDKGNPPLS STGTANVYVV DMNDHAPHIL YPSSTNSSAA FEMGPRTAPA
GYLVTKVIAM DSDSGQNAWL FYHLAQTSDL DLFKVELHTG EIRTTRKMGD ESGSTFNLTV
VVRDNGEPSL SASVAITVAV VDRVSKILPD TQRHVKSPRT YSEITLYLII ALSTVSFIFL
LTIIILSIIK CYRYTAYGTA CCGGFCGVRE RSPAELYKQA NNNIDARIPH GLKVQPHFIE
VRGNGSLTKT YCYKACLTAG SGSDTFMFYN TGAQTGPGPS GAQAAVTDSR NLTGQSGQNA
GNLIILKNEA VSQNEPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS
SATPEPEAGE VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP
ANSQIDKSDF ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
