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CDHR1_RAT
ID   CDHR1_RAT               Reviewed;         859 AA.
AC   Q91XU7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Cadherin-related family member 1;
DE   AltName: Full=MT-protocadherin;
DE   AltName: Full=Photoreceptor cadherin;
DE            Short=prCAD;
DE   AltName: Full=Protocadherin-21;
DE   Flags: Precursor;
GN   Name=Cdhr1; Synonyms=Kiaa1775, Pcdh21, Prcad;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
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   [2]
RP   TISSUE SPECIFICITY.
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 the retina. Strongly expressed by the
CC       mitral and tufted cells in the main and accessory olfactory bulbs. Also
CC       expressed in the septum and olfactory cortex. Weakly expressed in the
CC       triangular septal nucleus and piriform cortex.
CC       {ECO:0000269|PubMed:11597768, 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; AB053449; BAB61906.1; -; mRNA.
DR   RefSeq; NP_446024.1; NM_053572.1.
DR   AlphaFoldDB; Q91XU7; -.
DR   SMR; Q91XU7; -.
DR   STRING; 10116.ENSRNOP00000018631; -.
DR   GlyGen; Q91XU7; 4 sites.
DR   PaxDb; Q91XU7; -.
DR   GeneID; 93662; -.
DR   KEGG; rno:93662; -.
DR   UCSC; RGD:620420; rat.
DR   CTD; 92211; -.
DR   RGD; 620420; Cdhr1.
DR   VEuPathDB; HostDB:ENSRNOG00000013330; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_017357_0_0_1; -.
DR   InParanoid; Q91XU7; -.
DR   OMA; EAPQFIN; -.
DR   OrthoDB; 237790at2759; -.
DR   PhylomeDB; Q91XU7; -.
DR   PRO; PR:Q91XU7; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000013330; Expressed in thymus and 10 other tissues.
DR   Genevisible; Q91XU7; RN.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0008594; P:photoreceptor cell morphogenesis; ISO:RGD.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; ISO:RGD.
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; 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_0000318500"
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          789..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..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   859 AA;  93764 MW;  84FDB78609901C9B CRC64;
     MRRGPQVALV LGLLCIYLAQ ANFAPHFFDN GVGSTNGNMA LFSLPEDTPV GSHVYTLNGT
     DPEGDPISYH ISFDPSTRSV FSVDPNFGNI TLVEELDRER EDEIEAIISI SDGLNLVAEK
     VVIVVTDAND EAPRFLQEPY NILVPENTPA GSSIFKVQAE DKDTGSGGSV TYFLQSLHSS
     KFTVDRHSGV LRLQAGATLD YEKSRAHFIT VVAKDGGGRL RGADVVFSAT TTVTINVEDV
     QDTAPIFVGT PYYGYVYEDT LPGSEVLTVV AIDGDRGKPN HILYRLLNES DGLFEINETS
     GAISVLQSPA QLRREVYELH VQVTEVNSSG SPAAQSTVPV IIRIVDLNNH PPTFYGESGP
     QNKFELSMFE HPPQGEILRG LKITVNDSDQ GANAKFNLRL VGPGGIFRVV PQTVLNEAQV
     TIIVENSAAI DFEKSKSLTF KLLAIEVNTP EKFSSTADIV IQLLDTNDNV PKFTSHYYIA
     RIPENVPGGS NVVAVTAVDP DTGPWGKVQY SIYGTGSDLF LIHPSTGLIY TQPWASLDAE
     GTSRYNFYVK AEDMDGRYSL AEVFVTLLDV NDHYPQFVQS VQEKTMVLGT PLKIEATDQD
     AEEPNNLVDY SITRAEPVNV FDIDAHTGEI RLKNSIRSLE ALHNITPSGE YSWSLQVQAK
     DRGSPSFSTT ALLKIDITDT ERLSRSSMAA FLIQTKDNPM KAVGVLAGVM AIVVAITVLI
     STATFWRNKK SNKVLPVRRV LRRRPSPAPH TVRIEWLKFR RAKAASKFIL KEDPPNENCN
     NSRVGVTVPP RAPALPPPPK MASSTVAQQT VPTVSGSLTP QPSQQLPTPK PLGGPAQSSL
     VSELKQKFEK KSLGNKAYV
 
 
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