CDHR1_MOUSE
ID CDHR1_MOUSE Reviewed; 859 AA.
AC Q8VHP6; Q8CFQ4; Q8CH99;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=Kiaa1775, Pcdh21, Prcad;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=129;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [LARGE SCALE MRNA] OF 2-859.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, 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).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16106355; DOI=10.1002/gene.20146;
RA Nagai Y., Sano H., Yokoi M.;
RT "Transgenic expression of Cre recombinase in mitral/tufted cells of the
RT olfactory bulb.";
RL Genesis 43:12-16(2005).
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.
CC -!- SUBUNIT: Interacts with PROM1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VHP6; O43490: PROM1; Xeno; NbExp=3; IntAct=EBI-4395045, EBI-3447549;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. 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.
CC {ECO:0000269|PubMed:11738025, ECO:0000269|PubMed:15284225}.
CC -!- TISSUE SPECIFICITY: Expressed in cone and rod photoreceptor cells (at
CC protein level). Expressed in photoreceptor cells of the outer nuclear
CC layer of the retina. Expressed in mitral and tufted cells in the
CC olfactory bulb. {ECO:0000269|PubMed:11738025,
CC ECO:0000269|PubMed:15284225, ECO:0000269|PubMed:16106355}.
CC -!- PTM: Undergoes proteolytic cleavage; produces a soluble 95 kDa N-
CC terminal fragment and a 25 kDa cell-associated C-terminal fragment.
CC -!- DISRUPTION PHENOTYPE: Mice have no obvious phenotype but show
CC photoreceptor cell death as early as 1 month of age shortly after
CC completion of retinal development. Its absence severely compromises the
CC structure of OS which are disorganized and fragmented, but the
CC consequences on photoreceptor electrical signaling are very mild.
CC Proteolytic cleavage is partially inhibited in the absence of orderly
CC OS assembly in mouse retinas lacking RDS/peripherin.
CC {ECO:0000269|PubMed:11738025}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41482.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA.; Evidence={ECO:0000305};
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; AF426393; AAL65140.1; -; mRNA.
DR EMBL; BC042454; AAH42454.2; -; mRNA.
DR EMBL; BC058270; AAH58270.1; -; mRNA.
DR EMBL; AB093300; BAC41482.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS26952.1; -.
DR RefSeq; NP_570948.1; NM_130878.2.
DR AlphaFoldDB; Q8VHP6; -.
DR SMR; Q8VHP6; -.
DR IntAct; Q8VHP6; 1.
DR STRING; 10090.ENSMUSP00000022337; -.
DR GlyGen; Q8VHP6; 3 sites.
DR iPTMnet; Q8VHP6; -.
DR PhosphoSitePlus; Q8VHP6; -.
DR PaxDb; Q8VHP6; -.
DR PRIDE; Q8VHP6; -.
DR ProteomicsDB; 280035; -.
DR Antibodypedia; 30037; 67 antibodies from 21 providers.
DR DNASU; 170677; -.
DR Ensembl; ENSMUST00000022337; ENSMUSP00000022337; ENSMUSG00000021803.
DR GeneID; 170677; -.
DR KEGG; mmu:170677; -.
DR UCSC; uc007tbu.1; mouse.
DR CTD; 92211; -.
DR MGI; MGI:2157782; Cdhr1.
DR VEuPathDB; HostDB:ENSMUSG00000021803; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155509; -.
DR HOGENOM; CLU_017357_0_0_1; -.
DR InParanoid; Q8VHP6; -.
DR OMA; EAPQFIN; -.
DR OrthoDB; 237790at2759; -.
DR PhylomeDB; Q8VHP6; -.
DR TreeFam; TF332908; -.
DR BioGRID-ORCS; 170677; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cdhr1; mouse.
DR PRO; PR:Q8VHP6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8VHP6; protein.
DR Bgee; ENSMUSG00000021803; Expressed in pigmented layer of retina and 101 other tissues.
DR Genevisible; Q8VHP6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:BHF-UCL.
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:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; ISO:MGI.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISO:MGI.
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 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..859
FT /note="Cadherin-related family member 1"
FT /id="PRO_0000318499"
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..859
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 569..691
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 793..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
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 CONFLICT 578..579
FT /note="Missing (in Ref. 3; BAC41482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 94028 MW; 6D2BFFD9613325E9 CRC64;
MRRGPRVALV LGLLRIYLAQ ANFAPHFFDN GVGSTNGNMA LFSLPEDTPV GSHVYTLNGT
DPEGDPISYH ISFDPSTRSV FSVDPNFGNI TLVEELDRER EDEIEAIISI SDGLNLVAEK
VVILVTDAND EAPRFIQEPY IIRVPENIPA GSSIFKVQAE DKDTGSGGSV TYSLQNLHSS
KFSMDRHSGV LRLQAGATLD YEKSRAHYIT VIAKDGGGRL RGADMVFSAT TTVTINVEDV
QDTAPIFVGT PYYGYVYEDT LPGSEVLTVV AIDGDRGKPN HILYRLLNES DGIFEINETS
GAISVLQSPA LLRREVYELH VQVTEVNSPG SPAAQATVPV TIRIVDLNNH PPTFYGESGP
QNKFELSMFE HPPQGEILRG LKITVNDSDQ GANAKFNLRL VGPGGIFRVV PQTVLNEAQV
TIIVENSAAI DFEKSKLLTF KLLAIEVNTP EKFSSTADIV IQLLDTNDNV PKFTSHYYIA
RIPENAPGGS NVVAVTAVDP DTGPWGKVHY SIYGTGSDLF LIHPSTGLIY TQPWASLDAE
GTSRYNFYVK AEDMDGRYSL AEVFVTLLDV NDHYPQFVQS VQEKTMVLGT PLKIEATDQD
AEEPNNLVDY SITRAEPVNV FDIDAHTGEI RLKNSIRSLE ALHNITPSGD YSWSLQVQAK
DRGSPSFSTT ALLKIDITDT ERLSRGSMAA FLIQTKDNPM KAVGVLAGVM AIVVAITVLI
STATFWRNKK SNKVLPVRRV LRRRPSPAPH TVRIEWLKFR RAKAATKFIL KEDSPNENCN
NSRVGVMVPP RAPALPPPPK MASSMVAQQT VPTVSGSLTP QPSPQLPTPK TLGGPVQSSL
VSELKQKFEK KSLDNKAYI
