ID   CDHR1_XENLA             Reviewed;         867 AA.
AC   Q6B457;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15284225; DOI=10.1074/jbc.m407928200;
RA   Rattner A., Chen J., Nathans J.;
RT   "Proteolytic shedding of the extracellular domain of photoreceptor
RT   cadherin. Implications for outer segment assembly.";
RL   J. Biol. Chem. 279:42202-42210(2004).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in photoreceptor cells of the outer
CC       nuclear layer of the retina and in the pinal gland.
CC       {ECO:0000269|PubMed:15284225}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the retina 3 days post-fertilization
CC       (hpf). {ECO:0000269|PubMed:15284225}.
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DR   EMBL; AY683207; AAT91269.1; -; mRNA.
DR   RefSeq; NP_001165667.1; NM_001172196.1.
DR   AlphaFoldDB; Q6B457; -.
DR   SMR; Q6B457; -.
DR   GeneID; 100337587; -.
DR   KEGG; xla:100337587; -.
DR   CTD; 100337587; -.
DR   Xenbase; XB-GENE-865231; cdhr1.L.
DR   OrthoDB; 237790at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 100337587; Expressed in camera-type eye and 6 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..867
FT                   /note="Cadherin-related family member 1"
FT                   /id="PRO_0000318503"
FT   TOPO_DOM        22..707
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        708..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        729..867
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          39..138
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          139..250
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          251..357
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          363..476
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          477..580
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          572..692
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          777..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..811
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  95725 MW;  3EFC998DE392265C CRC64;
     MKHEWNLCPS IFFSIFHICL SVQTNYGPYF FDNGPGSTNG NMALLSLSED TPVGAYIYAL
     NGSDPDGDPV TFGLTFEPGS KRYFAVDPDN GNVTLIEELD REKQDEIEVI VSISDGINKV
     SEKVRVLVTD ANDESPGFLN TPYIVTVPED TPPGSSIFKI EAVDKDTGSG GSITYIIQEM
     HGSKFTIDRH SGVLRIKAGV SLDFEKSRTH FVSVLAKDGG GKLRGKNQVF TSTTTVTINV
     EDVQDSPPVF VGTPYYGYVY EDTTMGSEVL TVKAYDGDRG NPNTIYYSIV NGSDGAFTIN
     NATGGITVIK TPDELKKEVY ELKIQVSEIT PEGDKVAHAF TVATVRVVDL NNHPPTFYGE
     NGPQNRFELT MYEHPPEGEI LRGLKITVND SDQGANAKFN LRLVGPGGIF RVVPQTVLNE
     AQVTIIVENS AGIDYEKFHL FTFKLLAIEV NTPEKFSSTA DITIHLLDIN DNVPRFSSEY
     YIARIPENSP GGSNVVAATA TDLDSGLWGE IKYSIYGPGS DPFLIHPSTG IIYTQPWASL
     DAEVTSKYNF YVKAEDTEGK YSLAEVFVTV LDINDHSPEF SENIQEKTLI IGTPVKIEAT
     DHDAEEPNNI VDYSIMQADP SNVFDIDQST GEIKLKSYIR SLDIIQNITR NKDCKWSVVV
     QAKDRGSPSF STTAVVKIDV TEETLLHKGP MAAFLMQSKD NPMKALGVLA GVMAIMVVIT
     IFISTAMFWR NKKSNRVMPL RRIIKRRKND HPPRTARTEW LKFKKSNNSA DKFTIQEMES
     GPKNENRNNN YQGIPVPPRA PCPPPPPRLM PKVSKTERSL PTVSGSLTPK IIDQQMNERV
     PSASAALVSE LKQMLEKKNA GSSMSFY