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CRGC_RAT
ID   CRGC_RAT                Reviewed;         174 AA.
AC   P02529;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Gamma-crystallin C;
DE   AltName: Full=Gamma-C-crystallin;
DE   AltName: Full=Gamma-crystallin 2-1;
GN   Name=Crygc;
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.
RX   PubMed=3783678; DOI=10.1016/0022-2836(86)90379-7;
RA   den Dunnen J.T., Moormann R.J.M., Lubsen N.H., Schoenmakers J.G.G.;
RT   "Concerted and divergent evolution within the rat gamma-crystallin gene
RT   family.";
RL   J. Mol. Biol. 189:37-46(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2777080; DOI=10.1016/0378-1119(89)90223-0;
RA   den Dunnen J.T., van Neck J.W., Cremers F.P.M., Lubsen N.H.,
RA   Schoenmakers J.G.G.;
RT   "Nucleotide sequence of the rat gamma-crystallin gene region and comparison
RT   with an orthologous human region.";
RL   Gene 78:201-213(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-174.
RX   PubMed=6294661; DOI=10.1073/pnas.79.22.6876;
RA   Moormann R.J.M., den Dunnen J.T., Bloemendal H., Schoenmakers J.G.G.;
RT   "Extensive intragenic sequence homology in two distinct rat lens gamma-
RT   crystallin cDNAs suggests duplications of a primordial gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:6876-6880(1982).
CC   -!- FUNCTION: Crystallins are the dominant structural components of the
CC       vertebrate eye lens.
CC   -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC       Greek key motifs.
CC   -!- MISCELLANEOUS: There are six different gamma crystallins identified in
CC       rat lens.
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; M19359; AAA40983.1; -; Genomic_DNA.
DR   EMBL; J00717; AAA40986.1; -; mRNA.
DR   PIR; A02934; CYRTG2.
DR   PIR; C24060; C24060.
DR   PIR; I83432; I83432.
DR   RefSeq; NP_001075129.1; NM_001081660.1.
DR   AlphaFoldDB; P02529; -.
DR   SMR; P02529; -.
DR   STRING; 10116.ENSRNOP00000020078; -.
DR   iPTMnet; P02529; -.
DR   PhosphoSitePlus; P02529; -.
DR   PaxDb; P02529; -.
DR   GeneID; 24277; -.
DR   KEGG; rno:24277; -.
DR   UCSC; RGD:2421; rat.
DR   CTD; 1420; -.
DR   RGD; 2421; Crygc.
DR   InParanoid; P02529; -.
DR   OrthoDB; 1220704at2759; -.
DR   PhylomeDB; P02529; -.
DR   PRO; PR:P02529; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0001654; P:eye development; ISO:RGD.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEP:RGD.
DR   GO; GO:0007601; P:visual perception; ISO:RGD.
DR   InterPro; IPR001064; Beta/gamma_crystallin.
DR   InterPro; IPR011024; G_crystallin-like.
DR   Pfam; PF00030; Crystall; 2.
DR   PRINTS; PR01367; BGCRYSTALLIN.
DR   SMART; SM00247; XTALbg; 2.
DR   SUPFAM; SSF49695; SSF49695; 1.
DR   PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE   2: Evidence at transcript level;
KW   Eye lens protein; Methylation; Reference proteome; Repeat.
FT   CHAIN           1..174
FT                   /note="Gamma-crystallin C"
FT                   /id="PRO_0000057591"
FT   DOMAIN          2..40
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          41..83
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          88..128
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          129..171
FT                   /note="Beta/gamma crystallin 'Greek key' 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   REGION          84..87
FT                   /note="Connecting peptide"
FT   MOD_RES         23
FT                   /note="S-methylcysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16
FT                   /note="C -> S (in Ref. 1; no nucleotide entry and 3;
FT                   AAA40986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="I -> V (in Ref. 1; no nucleotide entry and 3;
FT                   AAA40986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="H -> R (in Ref. 3; AAA40986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="H -> Q (in Ref. 3; AAA40986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169..170
FT                   /note="RV -> SA (in Ref. 3; AAA40986)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  20951 MW;  ADB5D16DF57BC13B CRC64;
     MGKITFYEDR GFQGRCYECS SDCPNLQTYF SRCNSIRVDS GCWMLYERPN YQGHQYFLRR
     GDYPDYQQWM GFSDSIRSCR LIPHTGSHRM RLYEKEDHKG VMMELSEDCS CIQDRFHLSE
     VRSLHVLEGC WVLYEMPNYR GRQYLLRPQE YRRYHDWGAV DAKAGSLRRV VDLY
 
 
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