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CRGC_MOUSE
ID   CRGC_MOUSE              Reviewed;         174 AA.
AC   Q61597; Q03739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Gamma-crystallin C;
DE   AltName: Full=Gamma-C-crystallin;
GN   Name=Crygc; Synonyms=Gammab-cry;
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.
RC   STRAIN=102 X C3H; TISSUE=Liver;
RX   PubMed=8293998; DOI=10.1016/0378-1119(93)90458-f;
RA   Graw J., Liebstein A., Pietrowski D., Schmitt-John T., Werner T.;
RT   "Genomic sequences of murine gamma B- and gamma C-crystallin-encoding
RT   genes: promoter analysis and complete evolutionary pattern of mouse, rat
RT   and human gamma-crystallins.";
RL   Gene 136:145-156(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 OF 8-158.
RC   STRAIN=CD-1; TISSUE=Eye;
RX   PubMed=1623964; DOI=10.1016/0014-4835(92)90034-p;
RA   Goring D.R., Breitman M.L., Tsui L.-C.;
RT   "Temporal regulation of six crystallin transcripts during mouse lens
RT   development.";
RL   Exp. Eye Res. 54:785-795(1992).
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       mouse lens.
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; Z22574; CAA80297.1; -; Genomic_DNA.
DR   EMBL; BC056454; AAH56454.1; -; mRNA.
DR   EMBL; M64544; AAA53524.1; -; mRNA.
DR   CCDS; CCDS15012.1; -.
DR   PIR; I48360; S33526.
DR   PIR; I49614; I49614.
DR   RefSeq; NP_031801.1; NM_007775.2.
DR   PDB; 2V2U; X-ray; 1.90 A; A/B=2-174.
DR   PDBsum; 2V2U; -.
DR   AlphaFoldDB; Q61597; -.
DR   SMR; Q61597; -.
DR   STRING; 10090.ENSMUSP00000109698; -.
DR   PhosphoSitePlus; Q61597; -.
DR   PaxDb; Q61597; -.
DR   PRIDE; Q61597; -.
DR   ProteomicsDB; 284168; -.
DR   Antibodypedia; 34194; 176 antibodies from 27 providers.
DR   DNASU; 12966; -.
DR   Ensembl; ENSMUST00000027089; ENSMUSP00000027089; ENSMUSG00000025952.
DR   GeneID; 12966; -.
DR   KEGG; mmu:12966; -.
DR   UCSC; uc007bhi.2; mouse.
DR   CTD; 1420; -.
DR   MGI; MGI:88523; Crygc.
DR   VEuPathDB; HostDB:ENSMUSG00000025952; -.
DR   eggNOG; ENOG502RXJY; Eukaryota.
DR   GeneTree; ENSGT00940000159232; -.
DR   HOGENOM; CLU_081883_1_1_1; -.
DR   InParanoid; Q61597; -.
DR   BioGRID-ORCS; 12966; 1 hit in 72 CRISPR screens.
DR   EvolutionaryTrace; Q61597; -.
DR   PRO; PR:Q61597; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q61597; protein.
DR   Bgee; ENSMUSG00000025952; Expressed in lens of camera-type eye and 45 other tissues.
DR   ExpressionAtlas; Q61597; baseline and differential.
DR   Genevisible; Q61597; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0001654; P:eye development; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; ISO:MGI.
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   1: Evidence at protein level;
KW   3D-structure; Eye lens protein; Methylation; Reference proteome; Repeat.
FT   CHAIN           1..174
FT                   /note="Gamma-crystallin C"
FT                   /id="PRO_0000057597"
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   VARIANT         11
FT                   /note="S -> G (in strain: CD-1)"
FT   VARIANT         14
FT                   /note="G -> A (in strain: CD-1)"
FT   VARIANT         154..155
FT                   /note="FQ -> YH (in strain: CD-1)"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          13..21
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          35..48
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          99..107
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   HELIX           112..115
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:2V2U"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:2V2U"
SQ   SEQUENCE   174 AA;  20917 MW;  ECEF819F051D431D CRC64;
     MGKITFFEDR SFQGRCYECS SDCPNLQTYF SRCNSVRVDS GCWMLYERPN YQGHQYFLRR
     GEYPDYQQWM GFSDSIRSCR LIPHAGSHRM RLYEKEDHKG VMMELSEDCS CIQDRFHLSE
     VRSLQVLEGC WVLYEMPNYR GRQYLLRPQE YRRFQDWGSV DAKAGSLRRV VDLY
 
 
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