PCDC1_PANTR
ID PCDC1_PANTR Reviewed; 963 AA.
AC Q5DRE2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protocadherin alpha-C1;
DE Short=PCDH-alpha-C1;
DE Flags: Precursor;
GN Name=PCDHAC1;
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 RefSeq; NP_001076051.1; NM_001082582.1.
DR AlphaFoldDB; Q5DRE2; -.
DR SMR; Q5DRE2; -.
DR GeneID; 100034721; -.
DR KEGG; ptr:100034721; -.
DR CTD; 56135; -.
DR InParanoid; Q5DRE2; -.
DR OrthoDB; 64478at2759; -.
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; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030742; PCDHAC1.
DR PANTHER; PTHR24028:SF153; PTHR24028:SF153; 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; 5.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..963
FT /note="Protocadherin alpha-C1"
FT /id="PRO_0000003911"
FT TOPO_DOM 19..683
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..124
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 125..233
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 234..340
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 349..445
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 446..555
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..667
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 812..815
FT /note="PXXP 1"
FT REPEAT 845..848
FT /note="PXXP 2"
FT REPEAT 886..889
FT /note="PXXP 3"
FT REPEAT 904..907
FT /note="PXXP 4"
FT REGION 812..907
FT /note="4 X 4 AA repeats of P-X-X-P"
FT REGION 844..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 963 AA; 104053 MW; 0D062DA514478814 CRC64;
MVGWGVAVLC LWVSCGAAAG QLEYSVPEET ERGVAVGNLS ADLRLPAAAM SSRNFRFLSS
HRELYFGVDL PSGNLVVREP ADREQLCRAK AACVLTYDLV LEDPLELHKI RIHVLDTNDN
SPLFPAGDVQ LHIPEFLTPG ARFALPNAQD DDEGSNGILS YSLSPSQHFR LDMGSRVDGS
EYPELVLEKA LDREQRATHL LVLTARDGGL PARSGDAQVT IIVVDTNDNA PVFERSVYRT
KVPETAPNGT VLFRVQALDP DEGSNGEVQY SLSNSTQAEL RHRFHVHPKS GEVQVAASLG
PPETLLEAYI EARDEGVFGL ASTAKLLVEV TDVNDHAPEL DFLTLSNPVP EDAAPGTVIA
LFSVKDEDLD SNGRVICGMS SAGPFQLTAS FDNYYSLLID GPLDREQISE YQVLITASDS
GSPPLSTRRT ITVSVADVND NTPSFPQPQQ ELFIAENNGP GASLGRVFAQ DPDLGKNGLV
SYELLDVISE GPSASSLVAV ESSSGAITAK TSFDFEQLRG FHFQVEGRDG GIPPRSATVT
INLFVVDRND NYPVILFPLP RNCSVPVEIV PRSARTGHLV TKVVAEDADS GSNAWLSYHI
SRASDSSLFR ISANIGELRT ARLVLPTDAV KQRVVVVVRD HGDPPLSSSV TLGVLLSNSV
PQLLPDFEDV WEPGGQLSAQ NLYLVIALAC ISFLFLGCLL FFVCTKLHQS PGCCAQSCCR
STEDLRYGRK MVSNPCMTSA TIDVTTVERL SQTYLYRASL GLGSDNNSLL LRGEYNAADL
RNLATGVGLN LPISCIQIRN RKGDHANVNA MPRQPNPDWR YSASLRAGMH SSVHLEEAGI
LRAGPGGPDQ QWPTVSSATP EPEAGEVSPP VGAGVNSNSW TFKYGPGNPK QSGPGELPDK
FIIPGSPAII SIRQEPANSQ IDKSDFITFG KKEETKKKKK KKKGNKTQEK KEKGNSTTDN
SDQ
