PCDAB_PANTR
ID PCDAB_PANTR Reviewed; 949 AA.
AC Q5DRF3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protocadherin alpha-11;
DE Short=PCDH-alpha-11;
DE Flags: Precursor;
GN Name=PCDHA11;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; Q5DRF3; -.
DR SMR; Q5DRF3; -.
DR InParanoid; Q5DRF3; -.
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..949
FT /note="Protocadherin alpha-11"
FT /id="PRO_0000003905"
FT TOPO_DOM 30..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 157..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..349
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 350..454
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..564
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 580..677
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 733..736
FT /note="PXXP 1"
FT REPEAT 773..776
FT /note="PXXP 2"
FT REPEAT 795..798
FT /note="PXXP 3"
FT REPEAT 831..834
FT /note="PXXP 4"
FT REPEAT 872..875
FT /note="PXXP 5"
FT REPEAT 890..893
FT /note="PXXP 6"
FT REGION 733..893
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 753..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 949 AA; 103115 MW; 7C946E1F2D3A5BB3 CRC64;
MFGFQRRGLG TPRLQLWLLL LEFWEVGSGQ LHYSVSEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKT HGDLLEVNLQ NGILFVNSRI DREELCGQSA ECSIHLEVIV DRPLQVFHVN
VEVKDINDNP PVFSLREQKL LIAESKQSDS RFPLEGASDA DIEENALLTY RLSKNEYFSL
DSPTNGKQIK RLSLILKKSL DREKTPELNL MVTATDGGKP ELTGTVRLLV QVLDVNDNDP
DFDKSEYKVS LMENAAKETL VLKLNATDRD EGVNGEVTYS LMSIKPNGRH LFTLDQNNGE
VRVNGTLDYE ENKFYKIEVQ ATDKGTPPMA GHCTVWVEIL DTNDNSPEVA VTSLSLPVRE
DAQPSTVIAL ISVSDRDSGV NGQVTCSLTP HVPFKLVSTF KNYYSLVLDS ALDRESVWAY
ELVVTARDGG SPSLWATARV SVEVADVNDN APAFAQPEYT VFVKENNPPG CHIFTVSARD
ADAQENALVS YSLVERRLGD RALSSYVSVH AESGKVYALQ PLDHEELELL QFQVSARDAG
VPPLGSNVTL QVFVLDENDN APALLATQAG SAGGAVNKLV PRSVGAGHVV AKVRAVDADS
GYNAWLSYEL QPAAGGSRIP FRVGLYTGEI STTRALDEAD SPRHRLLVLV KDHGEPALTA
TATVLVSLVE SGQAPKASSR TLVGAASPEA ALVDVNVYLI IAICVVSSLL VLTLLLYTAL
WCSATPTEGA CAPGKPTLVC SRAVGSWSYS QQRRQRVCSE EGPPKTDLMA FSPSLPLGLN
KEEEGERQEP GSNHPGQPRQ PNPDWRYSAS LRAGMHSSVH LEEAGILRAG PGGPDQQWPT
VSSATPEPEA GEVSPPVGAG VNSNSWTFKY GPGNPKQSGP GELPDKFIIP GSPAIISIRQ
EPANSQIDKS DFITFGKKEE TKKKKKKKKG NKTQEKKEKG NSTTDNSDQ
