PCDA4_RAT
ID PCDA4_RAT Reviewed; 947 AA.
AC Q767I8; Q5U2Z9; Q8CJ01;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protocadherin alpha-4 {ECO:0000305};
DE Short=PCDH-alpha-4 {ECO:0000305};
DE AltName: Full=Cadherin-related neuronal receptor 4 {ECO:0000312|EMBL:BAD06369.1};
DE Flags: Precursor;
GN Name=Pcdha4 {ECO:0000312|RGD:620337};
GN Synonyms=Cnrv4 {ECO:0000303|PubMed:15028293};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Long Evans; TISSUE=Brain;
RX PubMed=15028293; DOI=10.1016/j.ygeno.2003.09.022;
RA Yanase H., Sugino H., Yagi T.;
RT "Genomic sequence and organization of the family of CNR/Pcdh genes in
RT rat.";
RL Genomics 83:717-726(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-512 (ISOFORMS 1/2).
RC STRAIN=Fischer 344;
RA Johnson K.J., Zecevic A., Kwon E.J.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination. Thereby, it is involved
CC in the establishment and maintenance of specific neuronal connections
CC in the brain. {ECO:0000250|UniProtKB:O88689}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells). Forms promiscuous heterodimers in cis (at the plasma
CC membrane of the same cell) with other protocadherins. Interacts with
CC FYN. {ECO:0000250|UniProtKB:O88689}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88689};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88689}.
CC Note=Detected in dendrites and synapses.
CC {ECO:0000250|UniProtKB:O88689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q767I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q767I8-2; Sequence=VSP_019416;
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:15028293}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell. This is a head-to-tail interaction, the cadherin
CC 1 domain interacting with the cadherin 4 domain and the cadherin 2
CC domain interacting the cadherin 3 domain of the other protocadherin.
CC The cadherin 6 domain mediates promiscuous interactions with
CC protocadherins on the same cell membrane. Each cadherin domain binds
CC three calcium ions. {ECO:0000250|UniProtKB:O88689}.
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 EMBL; AB113387; BAD06369.1; -; mRNA.
DR EMBL; BC085793; AAH85793.1; -; mRNA.
DR EMBL; AF539750; AAN31758.1; -; mRNA.
DR RefSeq; NP_446385.1; NM_053933.1. [Q767I8-1]
DR AlphaFoldDB; Q767I8; -.
DR SMR; Q767I8; -.
DR BioGRID; 250597; 1.
DR STRING; 10116.ENSRNOP00000067199; -.
DR GlyGen; Q767I8; 3 sites.
DR iPTMnet; Q767I8; -.
DR PhosphoSitePlus; Q767I8; -.
DR PaxDb; Q767I8; -.
DR PRIDE; Q767I8; -.
DR Ensembl; ENSRNOT00000079794; ENSRNOP00000075260; ENSRNOG00000020119. [Q767I8-1]
DR GeneID; 116741; -.
DR KEGG; rno:116741; -.
DR UCSC; RGD:620337; rat. [Q767I8-1]
DR CTD; 56144; -.
DR RGD; 620337; Pcdha4.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160554; -.
DR InParanoid; Q767I8; -.
DR OrthoDB; 64478at2759; -.
DR PRO; PR:Q767I8; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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:0042476; P:odontogenesis; NAS:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..947
FT /note="Protocadherin alpha-4"
FT /id="PRO_0000240664"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O88689"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O88689"
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 573..681
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 796..799
FT /note="PXXP 3"
FT REPEAT 829..832
FT /note="PXXP 4"
FT REPEAT 870..873
FT /note="PXXP 5"
FT REPEAT 888..891
FT /note="PXXP 6"
FT REGION 734..891
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 738..947
FT /note="Required for interaction with FYN"
FT /evidence="ECO:0000250|UniProtKB:O88689"
FT REGION 761..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
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"
FT DISULFID 96..102
FT /evidence="ECO:0000250|UniProtKB:O88689"
FT VAR_SEQ 535..795
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019416"
FT CONFLICT 69
FT /note="K -> R (in Ref. 3; AAN31758)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="R -> Q (in Ref. 3; AAN31758)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="V -> L (in Ref. 3; AAN31758)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="I -> H (in Ref. 3; AAN31758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 103042 MW; E6B9C3D9FAF2DD02 CRC64;
MEFSWGSGQE SQRLLLSFLF LAIWEPGNSQ LHYSIPEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKD RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV DRPLQVFHVE
VEVRDINDNP PTFPTTQKNL FIAESRPLDT WFPLEGASDS DIGINAVLTY RLSPNDYFSL
EKPTNSERVK GLGLILRKSL DREETPELFL VLTVTDGGKP ELTGSVQLLI TVLDANDNSP
VFDRSLYTVK LPENVPNGTL VVKVNASDLD EGANGEVMYS FSTDISPNVK NKFHIDPVTG
EIAVKGYIDF EECTSYEILI EGIDKGQLPL SGHCKVIVQV EDINDNAPEL EFKSLSLPIR
ENAPVGTVIA LISVFDPDTG VNGQVTCSLT PQVPFKLVST FKNYYSLVLD SALDRETTAD
YKVVVIARDG GLPSLWATAS VSVEVADVND NAPAFAQPEY TVFVKENNPP GAHIFTVSAV
DADSQENALV SYSLVERRVG ERLLSSYVSV HAESGKVFAL QPLDHEELEL LQFQVSARDA
GVPALGSNVT LQVFVLDEND NAPTLLEPEA GISGGIVSRL VSRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQSSEGNSRS LFRVGLYTGE ISTTRSLDEA DSPRQRLLVL VKDHGDPAMM
VTATVLVSLV ENGPLPKAPS RVSTRVTNAE ASLVDVNVYL IIAICAVSSL LVLTLLLYSA
LRCSTVPSES VCGPPKPVMV CSSAVGSWSY SQQRRQRVCS GEYPPKTDLM AFSPSLSDSR
DREDQLQSTE DSSGKPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS
SATPEPEAGE VSPPVGAGVN SNSWTFKYGP GNPKQPGPGE LPDKFIIPGS PAIISIRQES
ANNQIDKSDF ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
