CDHR1_BOVIN
ID CDHR1_BOVIN Reviewed; 867 AA.
AC Q8WN91;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cadherin-related family member 1;
DE AltName: Full=Photoreceptor cadherin;
DE Short=prCAD;
DE AltName: Full=Protocadherin-21;
DE Flags: Precursor;
GN Name=CDHR1; Synonyms=PCDH21, PRCAD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=11738025; DOI=10.1016/s0896-6273(01)00531-1;
RA Rattner A., Smallwood P.M., Williams J., Cooke C., Savchenko A.,
RA Lyubarsky A., Pugh E.N., Nathans J.;
RT "A photoreceptor-specific cadherin is essential for the structural
RT integrity of the outer segment and for photoreceptor survival.";
RL Neuron 32:775-786(2001).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC required for the structural integrity of the outer segment (OS) of
CC photoreceptor cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PROM1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Localized at the junction between the inner
CC and outer segments of rod and cone photoreceptors cells. Confined to
CC the base of the OS. Localized on the edges of nascent evaginating disks
CC on the side of the OS opposite the connecting cilium. Expressed at
CC postnatal day 2 at the apical tip of the rod photoreceptor cells, the
CC site of the developing OS. Colocalized with rhodopsin between postnatal
CC days 2 and 9 at the base of the growing OS region (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in photoreceptor cells of the outer
CC nuclear layer of the retina. {ECO:0000269|PubMed:11738025}.
CC -!- PTM: Undergoes proteolytic cleavage; produces a soluble 95 kDa N-
CC terminal fragment and a 25 kDa cell-associated C-terminal fragment.
CC {ECO:0000250}.
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DR EMBL; AF426392; AAL65139.1; -; mRNA.
DR RefSeq; NP_777248.1; NM_174823.2.
DR AlphaFoldDB; Q8WN91; -.
DR SMR; Q8WN91; -.
DR STRING; 9913.ENSBTAP00000001628; -.
DR PaxDb; Q8WN91; -.
DR GeneID; 281996; -.
DR KEGG; bta:281996; -.
DR CTD; 92211; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q8WN91; -.
DR OrthoDB; 237790at2759; -.
DR Proteomes; UP000009136; 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:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Vision.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..867
FT /note="Cadherin-related family member 1"
FT /id="PRO_0000318497"
FT TOPO_DOM 22..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..247
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 248..354
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 360..473
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 474..577
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 574..689
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 767..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 867 AA; 94290 MW; 042B3FDFB615FEAF CRC64;
MGRGPPAVLA PWMLFLSLAQ ANFAPHFFDN GAGSTNGNMA LFSLPEDTPV GSHVYTLNGT
DPEGDPVSYH ISFNPSARSV FSVDPNLGNI TLIEELDRER EDEIEAIISI SDGLNLVAEK
VTILVTDAND EAPRFIQEPY VVQVPEDTPS GSSIARVRAV DRDTGSAGSV TYFLKNPHPT
EFSVDRHSGV LRLRAGAILD FEKARAHFVT VVAKDGGGKL RGADVVLSAT TVVTVNVEDV
QDMGPVFVGT PYYGYVYEDT LPGSEVLMVV AMDGDRGKPN RVLYSLVNGS DGAFEINETS
GAISVMQSPS QLRREVYELH VQVTEVSSAG TPAAQAMVPV TIRIVDLNNH PPTFYGESGP
QNRFELSMYE HPPQGEILRG LKITVNDSDQ GANAKFNLRL VGPGGIFRVV PQTVLNEAQV
TIIVENSAAI DFEKSKVLTF KLLAIEVNTP EKFSSTADVV IQLLDTNDNV PKFTSHYYVA
RIPENAPGGS NVLAVTAVDP DSGPWGEVKY SIYGSGADLF LIHPSSGIIY TQPWASLDAE
ATARYNFYVK AEDMEGRYSL AEVFITLLDV NDHYPQFGKS VQEKTMVLGT PVKIEATDQD
AEEPNNLVDY SITHAEPANV FDINAHTGEI WLKNSIRSLD ALHNITPSGD RTWSLEVQAK
DRGSPSFSTT ALLKIDIVDT EMLSRSPMAA FLMQTKDNPM KAVGVLAGIM AIIVAITVLI
STATFWRNKK SNKVQPVRRV LRKRPSPAPR SVRIEWLKFR RTKAADKFVL REAPPNENCN
NNSRGSTPAP QAPAPPPPPS PAPSVGQAPW TVPTVSGSLA PQQPQQPSPK PRAVAKRKAV
GSPVQSALVS ELRQKFEKKN LHSKAYF
