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CDHR1_HUMAN
ID   CDHR1_HUMAN             Reviewed;         859 AA.
AC   Q96JP9; Q69YZ8; Q8IXY5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Cadherin-related family member 1 {ECO:0000305};
DE   AltName: Full=Photoreceptor cadherin;
DE            Short=prCAD;
DE   AltName: Full=Protocadherin-21;
DE   Flags: Precursor;
GN   Name=CDHR1 {ECO:0000312|HGNC:HGNC:14550}; Synonyms=KIAA1775, PCDH21, PRCAD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retinoblastoma;
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 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11597768; DOI=10.1016/s0169-328x(01)00218-2;
RA   Nakajima D., Nakayama M., Kikuno R., Hirosawa M., Nagase T., Ohara O.;
RT   "Identification of three novel non-classical cadherin genes through
RT   comprehensive analysis of large cDNAs.";
RL   Brain Res. Mol. Brain Res. 94:85-95(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-859 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   INTERACTION WITH PROM1.
RX   PubMed=18654668; DOI=10.1172/jci35891;
RA   Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M.,
RA   Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., Al-Sheikh Y.T.,
RA   Karan G., Corbeil D., Escher P., Kamaya S., Li C., Johnson S.,
RA   Frederick J.M., Zhao Y., Wang C., Cameron D.J., Huttner W.B.,
RA   Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., Baehr W., Hunt D.M.,
RA   Williams D.S., Zhang K.;
RT   "Mutant prominin 1 found in patients with macular degeneration disrupts
RT   photoreceptor disk morphogenesis in mice.";
RL   J. Clin. Invest. 118:2908-2916(2008).
RN   [6]
RP   INVOLVEMENT IN CORD15.
RX   PubMed=20805371; DOI=10.1136/jmg.2009.069120;
RA   Ostergaard E., Batbayli M., Duno M., Vilhelmsen K., Rosenberg T.;
RT   "Mutations in PCDH21 cause autosomal recessive cone-rod dystrophy.";
RL   J. Med. Genet. 47:665-669(2010).
RN   [7]
RP   VARIANTS THR-212 AND ALA-532.
RX   PubMed=16288196;
RA   Bolz H., Ebermann I., Gal A.;
RT   "Protocadherin-21 (PCDH21), a candidate gene for human retinal
RT   dystrophies.";
RL   Mol. Vis. 11:929-933(2005).
RN   [8]
RP   VARIANT CORD15 ALA-574.
RX   PubMed=26350383; DOI=10.1038/srep13902;
RA   Nikopoulos K., Avila-Fernandez A., Corton M., Lopez-Molina M.I.,
RA   Perez-Carro R., Bontadelli L., Di Gioia S.A., Zurita O.,
RA   Garcia-Sandoval B., Rivolta C., Ayuso C.;
RT   "Identification of two novel mutations in CDHR1 in consanguineous Spanish
RT   families with autosomal recessive retinal dystrophy.";
RL   Sci. Rep. 5:13902-13902(2015).
RN   [9]
RP   VARIANT SER-716.
RX   PubMed=28965847; DOI=10.1016/j.ajhg.2017.08.017;
RA   De Mori R., Romani M., D'Arrigo S., Zaki M.S., Lorefice E., Tardivo S.,
RA   Biagini T., Stanley V., Musaev D., Fluss J., Micalizzi A., Nuovo S.,
RA   Illi B., Chiapparini L., Di Marcotullio L., Issa M.Y., Anello D.,
RA   Casella A., Ginevrino M., Leggins A.S., Roosing S., Alfonsi R., Rosati J.,
RA   Schot R., Mancini G.M.S., Bertini E., Dobyns W.B., Mazza T., Gleeson J.G.,
RA   Valente E.M.;
RT   "Hypomorphic Recessive Variants in SUFU Impair the Sonic Hedgehog Pathway
RT   and Cause Joubert Syndrome with Cranio-facial and Skeletal Defects.";
RL   Am. J. Hum. Genet. 101:552-563(2017).
RN   [10]
RP   VARIANT SER-171.
RX   PubMed=30120214; DOI=10.1136/jmedgenet-2018-105364;
RA   de Bruijn S.E., Verbakel S.K., de Vrieze E., Kremer H., Cremers F.P.M.,
RA   Hoyng C.B., van den Born L.I., Roosing S.;
RT   "Homozygous variants in KIAA1549, encoding a ciliary protein, are
RT   associated with autosomal recessive retinitis pigmentosa.";
RL   J. Med. Genet. 55:705-712(2018).
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:0000269|PubMed:18654668}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96JP9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96JP9-2; Sequence=VSP_031190, VSP_031191;
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}.
CC   -!- DISEASE: Cone-rod dystrophy 15 (CORD15) [MIM:613660]: An inherited
CC       retinal dystrophy characterized by retinal pigment deposits visible on
CC       fundus examination, predominantly in the macular region, and initial
CC       loss of cone photoreceptors followed by rod degeneration. This leads to
CC       decreased visual acuity and sensitivity in the central visual field,
CC       followed by loss of peripheral vision. Severe loss of vision occurs
CC       earlier than in retinitis pigmentosa, due to cone photoreceptors
CC       degenerating at a higher rate than rod photoreceptors.
CC       {ECO:0000269|PubMed:20805371, ECO:0000269|PubMed:26350383}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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DR   EMBL; AC022389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038799; AAH38799.1; -; mRNA.
DR   EMBL; AB053448; BAB61905.1; -; mRNA.
DR   EMBL; AL080188; CAH10732.1; -; mRNA.
DR   CCDS; CCDS53548.1; -. [Q96JP9-2]
DR   CCDS; CCDS7372.1; -. [Q96JP9-1]
DR   RefSeq; NP_001165442.1; NM_001171971.2. [Q96JP9-2]
DR   RefSeq; NP_149091.1; NM_033100.3. [Q96JP9-1]
DR   AlphaFoldDB; Q96JP9; -.
DR   SMR; Q96JP9; -.
DR   BioGRID; 124919; 5.
DR   IntAct; Q96JP9; 2.
DR   STRING; 9606.ENSP00000485478; -.
DR   GlyGen; Q96JP9; 4 sites.
DR   iPTMnet; Q96JP9; -.
DR   PhosphoSitePlus; Q96JP9; -.
DR   BioMuta; CDHR1; -.
DR   DMDM; 166980558; -.
DR   jPOST; Q96JP9; -.
DR   MassIVE; Q96JP9; -.
DR   PaxDb; Q96JP9; -.
DR   PeptideAtlas; Q96JP9; -.
DR   PRIDE; Q96JP9; -.
DR   ProteomicsDB; 77001; -. [Q96JP9-1]
DR   ProteomicsDB; 77002; -. [Q96JP9-2]
DR   Antibodypedia; 30037; 67 antibodies from 21 providers.
DR   DNASU; 92211; -.
DR   Ensembl; ENST00000332904.7; ENSP00000331063.3; ENSG00000148600.15. [Q96JP9-2]
DR   Ensembl; ENST00000623527.4; ENSP00000485478.1; ENSG00000148600.15. [Q96JP9-1]
DR   GeneID; 92211; -.
DR   KEGG; hsa:92211; -.
DR   MANE-Select; ENST00000623527.4; ENSP00000485478.1; NM_033100.4; NP_149091.1.
DR   UCSC; uc001kcv.4; human. [Q96JP9-1]
DR   CTD; 92211; -.
DR   DisGeNET; 92211; -.
DR   GeneCards; CDHR1; -.
DR   HGNC; HGNC:14550; CDHR1.
DR   HPA; ENSG00000148600; Group enriched (retina, skin).
DR   MalaCards; CDHR1; -.
DR   MIM; 609502; gene.
DR   MIM; 613660; phenotype.
DR   neXtProt; NX_Q96JP9; -.
DR   OpenTargets; ENSG00000148600; -.
DR   Orphanet; 1872; Cone rod dystrophy.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA33005; -.
DR   VEuPathDB; HostDB:ENSG00000148600; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000155509; -.
DR   HOGENOM; CLU_017357_0_0_1; -.
DR   InParanoid; Q96JP9; -.
DR   OMA; HYEIALF; -.
DR   OrthoDB; 237790at2759; -.
DR   PhylomeDB; Q96JP9; -.
DR   TreeFam; TF332908; -.
DR   PathwayCommons; Q96JP9; -.
DR   SignaLink; Q96JP9; -.
DR   BioGRID-ORCS; 92211; 8 hits in 1066 CRISPR screens.
DR   ChiTaRS; CDHR1; human.
DR   GenomeRNAi; 92211; -.
DR   Pharos; Q96JP9; Tbio.
DR   PRO; PR:Q96JP9; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96JP9; protein.
DR   Bgee; ENSG00000148600; Expressed in upper arm skin and 115 other tissues.
DR   ExpressionAtlas; Q96JP9; baseline and differential.
DR   Genevisible; Q96JP9; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
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:UniProtKB.
DR   GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:UniProtKB.
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   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Cone-rod dystrophy; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..859
FT                   /note="Cadherin-related family member 1"
FT                   /id="PRO_0000318498"
FT   TOPO_DOM        20..700
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        722..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..246
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          247..353
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          359..472
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          473..576
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          573..688
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          770..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..818
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        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         681..744
FT                   /note="TLSRSPMAAFLIQTKDNPMKAVGVLAGTMATVVAITVLISTATFWRNKKSNK
FT                   VLPMRRVLRKRP -> VRRLRYMKNSNFPGTTKSVRKPKFKPKKPHSSQGLFLHPHCEI
FT                   ALFNLSNVNLYSRVFQGAAQAS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031190"
FT   VAR_SEQ         745..859
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031191"
FT   VARIANT         53
FT                   /note="H -> Q (in dbSNP:rs12781048)"
FT                   /id="VAR_038744"
FT   VARIANT         171
FT                   /note="T -> S (in dbSNP:rs759855253)"
FT                   /evidence="ECO:0000269|PubMed:30120214"
FT                   /id="VAR_083318"
FT   VARIANT         212
FT                   /note="A -> T (in dbSNP:rs200880106)"
FT                   /evidence="ECO:0000269|PubMed:16288196"
FT                   /id="VAR_038745"
FT   VARIANT         243
FT                   /note="A -> V (in dbSNP:rs7086200)"
FT                   /id="VAR_038746"
FT   VARIANT         532
FT                   /note="P -> A (in dbSNP:rs143662988)"
FT                   /evidence="ECO:0000269|PubMed:16288196"
FT                   /id="VAR_038747"
FT   VARIANT         574
FT                   /note="P -> A (in CORD15)"
FT                   /evidence="ECO:0000269|PubMed:26350383"
FT                   /id="VAR_075501"
FT   VARIANT         716
FT                   /note="T -> S (found in a patient with Joubert syndrome;
FT                   unknown pathological significance)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080429"
SQ   SEQUENCE   859 AA;  93595 MW;  7D5D9E3E3353039A CRC64;
     MRRCRWAALA LGLLRLCLAQ ANFAPHFFDN GVGSTNGNMA LFSLPEDTPV GSHVYTLNGT
     DPEGDPISYH ISFDPSTRSV FSVDPTFGNI TLVEELDRER EDEIEAIISI SDGLNLVAEK
     VVILVTDAND EAPRFIQEPY VALVPEDIPA GSIIFKVHAV DRDTGSGGSV TYFLQNLHSP
     FAVDRHSGVL RLQAGATLDY ERSRTHYITV VAKDGGGRLH GADVVFSATT TVTVNVEDVQ
     DMAPVFVGTP YYGYVYEDTL PGSEVLKVVA MDGDRGKPNR ILYSLVNGND GAFEINETSG
     AISITQSPAQ LQREVYELHV QVTEMSPAGS PAAQATVPVT IRIVDLNNHP PTFYGESGPQ
     NRFELSMNEH PPQGEILRGL KITVNDSDQG ANAKFNLQLV GPRGIFRVVP QTVLNEAQVT
     IIVENSAAID FEKSKVLTFK LLAVEVNTPE KFSSTADVVI QLLDTNDNVP KFDSLYYVAR
     IPENAPGGSS VVAVTAVDPD TGPWGEVKYS TYGTGADLFL IHPSTGLIYT QPWASLDAEA
     TARYNFYVKA EDMEGKYSVA EVFITLLDVN DHPPQFGKSV QKKTMVLGTP VKIEAIDEDA
     EEPNNLVDYS ITHAEPANVF DINSHTGEIW LKNSIRSLDA LHNITPGRDC LWSLEVQAKD
     RGSPSFSTTA LLKIDITDAE TLSRSPMAAF LIQTKDNPMK AVGVLAGTMA TVVAITVLIS
     TATFWRNKKS NKVLPMRRVL RKRPSPAPRT IRIEWLKSKS TKAATKFMLK EKPPNENCNN
     NSPESSLLPR APALPPPPSV APSTGAAQWT VPTVSGSLTP QPTQPPPKPK TMGSPVQSTL
     ISELKQKFEK KSVHNKAYF
 
 
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