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Database: UniProt
Entry: A0A0G2JG52_MOUSE
LinkDB: A0A0G2JG52_MOUSE
Original site: A0A0G2JG52_MOUSE 
ID   A0A0G2JG52_MOUSE        Unreviewed;      2065 AA.
AC   A0A0G2JG52;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Crystallin beta-gamma domain containing 1 {ECO:0000313|Ensembl:ENSMUSP00000143429.2};
GN   Name=Crybg1 {ECO:0000313|Ensembl:ENSMUSP00000143429.2,
GN   ECO:0000313|MGI:MGI:109544};
GN   Synonyms=Aim1 {ECO:0000313|MGI:MGI:109544};
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 {ECO:0000313|Ensembl:ENSMUSP00000143429.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000143429.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000143429.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000143429.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000143429.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family.
CC       {ECO:0000256|ARBA:ARBA00009646}.
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DR   RefSeq; XP_006512561.1; XM_006512498.3.
DR   AlphaFoldDB; A0A0G2JG52; -.
DR   SMR; A0A0G2JG52; -.
DR   ProteomicsDB; 373575; -.
DR   Antibodypedia; 70882; 26 antibodies from 9 providers.
DR   Ensembl; ENSMUST00000200401.2; ENSMUSP00000143429.2; ENSMUSG00000019866.16.
DR   AGR; MGI:109544; -.
DR   MGI; MGI:109544; Crybg1.
DR   VEuPathDB; HostDB:ENSMUSG00000019866; -.
DR   eggNOG; ENOG502QUA4; Eukaryota.
DR   GeneTree; ENSGT00940000155695; -.
DR   InParanoid; A0A0G2JG52; -.
DR   OMA; WEAMVLT; -.
DR   OrthoDB; 5354696at2759; -.
DR   BioGRID-ORCS; 11630; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Crybg1; mouse.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; A0A0G2JG52; Protein.
DR   Bgee; ENSMUSG00000019866; Expressed in substantia propria of cornea and 133 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JG52; baseline and differential.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0001654; P:eye development; IEA:UniProt.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.60.20.10; Crystallins; 6.
DR   InterPro; IPR001064; Beta/gamma_crystallin.
DR   InterPro; IPR011024; G_crystallin-like.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11818; BETA/GAMMA CRYSTALLIN; 1.
DR   PANTHER; PTHR11818:SF2; BETA_GAMMA CRYSTALLIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00030; Crystall; 6.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR01367; BGCRYSTALLIN.
DR   SMART; SM00458; RICIN; 1.
DR   SMART; SM00247; XTALbg; 6.
DR   SUPFAM; SSF49695; gamma-Crystallin-like; 3.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 9.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:A0A0G2JG52,
KW   ECO:0007829|MaxQB:A0A0G2JG52};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1408..1461
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1508..1550
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1562..1614
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1615..1657
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1706..1748
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1759..1796
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1797..1840
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1846..1886
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   DOMAIN          1887..1928
FT                   /note="Beta/gamma crystallin 'Greek key'"
FT                   /evidence="ECO:0000259|PROSITE:PS50915"
FT   REGION          1..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1212..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..737
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..974
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1283..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2065 AA;  223448 MW;  8E803277F74185EF CRC64;
     MPLSPPSQGD PREASPSKAP KKHPTFHIWR SKKKQSPSSS CGVFIPHPPG AFGETRAFLV
     PDGSQGEPQE LTLHGGELQL SDTPSEVPGP SSTESAMLKK SRAQPPEDTR RKPVLEKLGT
     LFTAGRRRNT RNGLESPTNS NSKSASAKVP KTGSEKTKAQ DNQLKATDAG EAGPRQEAEG
     QPVESCVQAT PCDAEQSPCS SINVGVVQQC HSNDSAQLEP LQAEGETFPD ATTAAKELLH
     SSPGNRSRQE SAETPARSPG EEALPGAGLQ PETARGVSGS PPEEHLVGGV GEAPDGAPGV
     GAEAGSLGAP GDAVPPGEPP AQDAETSRTA GSVDRAHPTK VLTLDIYLSK TEVAQVDEPA
     SIAPGTDDCE DSDDMEKRSS GRRSGRRRKS QKSTDSPGAD AVAPESAAKD EAVFDDEVAP
     DAAAENCLAE RKVKSVQAVP DGGAAPVACP EPKASSCPRG QPRGEPDRSK PLSPTKRKGR
     SRVPEAVPSS PGSGSRAPAK ESPPKRAPAA ADSGEEAGRV VPRELTVKSS SLLPEIKPEH
     KRGPLPHHFD SRGDGGRSRG TGASDADGLK PRNQFGVGRS TVTTKVTLPA RPKHVELNLK
     TPKNPDSLGN EHNSFSQPVH KGNTANKISL FENKRANSSP RHPDVRNTRN NPPSSKTFVG
     RAKLNLAKKA KEMEQPEKKA VSTSHQNGLV VKEPSAEGKG TAVPVPREEI RPATRGGEGE
     STKDQVLRPE PEQSDKLDVQ TDTAYPSHPG PTALVPVKDS ELSGEGQPEA ADSKGPVLNN
     TSDVAQDIAA ICDAREAPPK PQDAFSDSQP ASAAESARES SLPPSAPISV DAPQDGCVQV
     PICSVPCTAL EVSENHNGCV SPVSPHTEKT PISKPGVGEA SPPSTPEHSP ETMGKDCPSK
     VLVQVRSFVL PVENPQDVSS QVISESSEVR EAQLPSCHSN EPEVVSVTTC VPQHEDAPDT
     SPKDIHHREG HVAQSRPHIT QSGPEKAPPI QSSSGMPQTA EFILTHSPSS RSHAEGPQRP
     GQDATSPLTP TRLLNISAGS DNSVLDSSSD MEKFTEIIKK MDSAVCVPQK KKKARVPNSP
     APHFAMPPIH EDSLEKVFDP NVFTIGLGKK KESLAEVSPA LHLLQNHDPI SKLRAKRAST
     EQSIVFKSLH TNSNGKSEPQ TTSEASDKEN RDINSGGVKR SRLENSTLFS SMLSSLPQDK
     VFSPSVTSVN TMSTSFSTSQ NSSVSQSSVV QPRKEGGLPC GSDKEQPHLA PHNSLKVFNF
     NSSNTSRLGS SHMEKYPQKE GSKEDVNSQG NLQLPENNLS DLPKLKNSDG VEGILKSNLP
     NVGSVDADFL GLFKASRYDP GHSFSGMSLS DSMTLRGSMH SKLNPRPGKV VIFSEPDVSE
     ECIEVFGDIQ DCSSWRLSPV IVVKVVRGCW ILYEKANFEG HSLALEEGEL ELSSIWGTEE
     MLDEEAESDK PVVIGSIRHV VQDYRISQID LFTEPEGLGL LNSYFDDTEE MQGFPVMQKT
     CSIKVHWGTW LIYEEPGFQG VPFILEPGEY PDLSFWDTEE AYIGSMRPLK MGGRKVEFPT
     DPKVVIYEKP SFEGRCMELE TEMSSFIMEG GETEETTGNN NLPFTSVGSM KVLRGVWVAY
     EKCGFTGHQY LLEEGEYRDW NAWGGYNGEL QSLRPILSDF SNAHMIMYSE KNFGSKGSSI
     DVLGIVANLK ETGYGVKTQS INVLSGVWVA YENPDFTGEQ YVLDKGFYTS FEDWGGKNCK
     ISSVQPICLD SFTGPRRRNQ IHLFSEPQFQ GQSQSFEETI DQIDDSFQTK SCRVLGGSWV
     AYDGENFSGN QYVLEEGHYP CLSAMGCLPG ATLKSLRFID FEFSEPTIIL FERENFKGKK
     IELNAETVNL RSLGFNTQIR SVRVVGGIWV TYEYGNYRGR QFLLSPAEVP NWYEFSACRQ
     IGSLRPFAQK RIYFRLRNKA TGLFMSTNGN LEDLKLLRVQ VMEDVGADDQ IWIYQEGCIK
     CRIAEDCCLT IVGSLVTSGS KLGLALDQNV DSQFWCMKSD GRIYSKMKPN LVLDVKGGAQ
     YDQNHIILNT VSTEKLTQVW EAMVL
//
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