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CRBG3_MOUSE
ID   CRBG3_MOUSE             Reviewed;        1005 AA.
AC   Q80W49; Q3TRS6; Q8BMQ9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Beta/gamma crystallin domain-containing protein 3;
GN   Name=Crybg3;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 619-1005 (ISOFORM 1/2/3).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-129; SER-130;
RP   SER-136 AND SER-140, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, and Testis;
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 510-601.
RX   PubMed=23043265; DOI=10.1021/bi300844u;
RA   Rajanikanth V., Srivastava S.S., Singh A.K., Rajyalakshmi M., Chandra K.,
RA   Aravind P., Sankaranarayanan R., Sharma Y.;
RT   "Aggregation-prone near-native intermediate formation during unfolding of a
RT   structurally similar nonlenticular betagamma-crystallin domain.";
RL   Biochemistry 51:8502-8513(2012).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80W49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80W49-2; Sequence=VSP_032388;
CC       Name=3;
CC         IsoId=Q80W49-3; Sequence=VSP_032387, VSP_032389;
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; AK030282; BAC26878.1; -; mRNA.
DR   EMBL; AK162506; BAE36951.1; -; mRNA.
DR   EMBL; AC154473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043118; AAH43118.1; -; mRNA.
DR   RefSeq; NP_777273.2; NM_174848.3.
DR   PDB; 4FD9; X-ray; 1.86 A; A/B=510-601.
DR   PDBsum; 4FD9; -.
DR   AlphaFoldDB; Q80W49; -.
DR   SMR; Q80W49; -.
DR   STRING; 10090.ENSMUSP00000037682; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   iPTMnet; Q80W49; -.
DR   PhosphoSitePlus; Q80W49; -.
DR   EPD; Q80W49; -.
DR   MaxQB; Q80W49; -.
DR   PaxDb; Q80W49; -.
DR   PeptideAtlas; Q80W49; -.
DR   PRIDE; Q80W49; -.
DR   ProteomicsDB; 285302; -. [Q80W49-1]
DR   ProteomicsDB; 285303; -. [Q80W49-2]
DR   ProteomicsDB; 285304; -. [Q80W49-3]
DR   GeneID; 224273; -.
DR   KEGG; mmu:224273; -.
DR   UCSC; uc007zpj.2; mouse. [Q80W49-3]
DR   UCSC; uc007zpk.2; mouse. [Q80W49-2]
DR   CTD; 131544; -.
DR   MGI; MGI:2676311; Crybg3.
DR   eggNOG; ENOG502QTHR; Eukaryota.
DR   HOGENOM; CLU_002147_1_0_1; -.
DR   InParanoid; Q80W49; -.
DR   OrthoDB; 89929at2759; -.
DR   BioGRID-ORCS; 224273; 0 hits in 51 CRISPR screens.
DR   ChiTaRS; Crybg3; mouse.
DR   PRO; PR:Q80W49; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80W49; protein.
DR   Genevisible; Q80W49; MM.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR   GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR   CDD; cd00161; RICIN; 1.
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   Pfam; PF00030; Crystall; 6.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR01367; BGCRYSTALLIN.
DR   SMART; SM00458; RICIN; 1.
DR   SMART; SM00247; XTALbg; 5.
DR   SUPFAM; SSF49695; SSF49695; 3.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 7.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Lectin; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1005
FT                   /note="Beta/gamma crystallin domain-containing protein 3"
FT                   /id="PRO_0000325759"
FT   DOMAIN          367..416
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          462..500
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          512..556
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          557..599
FT                   /note="Beta/gamma crystallin 'Greek key' 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          605..647
FT                   /note="Beta/gamma crystallin 'Greek key' 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          648..690
FT                   /note="Beta/gamma crystallin 'Greek key' 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          701..737
FT                   /note="Beta/gamma crystallin 'Greek key' 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          738..781
FT                   /note="Beta/gamma crystallin 'Greek key' 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          828..869
FT                   /note="Beta/gamma crystallin 'Greek key' 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          871..1003
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          132..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..698
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032387"
FT   VAR_SEQ         1
FT                   /note="M -> MEVAMERTNGTTPGVTIMQTDALGPAFENTKDPREYMEKSIGEIEEP
FT                   PGEVKKGLILHDDRLASHFRGYESPTLSKDYEGYPASAIPDVQEEDTVVRLKKIM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032388"
FT   VAR_SEQ         699..702
FT                   /note="PTHL -> MFSQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032389"
FT   STRAND          513..519
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   HELIX           520..522
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          523..531
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   HELIX           536..539
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          551..557
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          559..564
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   TURN            565..567
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          568..574
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          576..579
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   TURN            582..584
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   HELIX           586..589
FT                   /evidence="ECO:0007829|PDB:4FD9"
FT   STRAND          594..597
FT                   /evidence="ECO:0007829|PDB:4FD9"
SQ   SEQUENCE   1005 AA;  114262 MW;  445C6ED46D2614A6 CRC64;
     MSVPVVYDKR RNLDCREEKE ESNLAFVSQD EQDSSSFTIL YEEPLQEEDR YTSAELRGSQ
     SLLFPDTSSM PGLACERSES RTDLVHHFEK EGKLGEAFDG DNSEMFLSVE AKRYKIYPLA
     LSPIYEDDSS QEDVLSSEVS PGHHGSSKSR ESANQPSSVL SLLQSVSERL QRNFDGDDRQ
     EAEEEEEEAV ASGKDWRTEK REHVTFHLPD PSIPFYPEDN QEHAGIFKSY VEFSEPTTSS
     LQHGRWSEKE LFLQKSDMTS KLHSSLKSAY HQYLQTSRTH SSETGTRFGG TLQEPVSKYF
     RVQDHAGRLS PYVENVDKQT LKCNPRPGKM IIYDLHGSKY KQEVYCNIPD ATTWSFPNGA
     LIKVVRGCWI LYEKPHFQGQ KCVLEEGERV LDRDWLLQNR KHPERNFVLG SIKRVLKDCS
     IPVIELCPKT DPGCSPIYIH RSVPNVEELN IPKSTSVTVK SGVWLAYPDI HFKGQATILE
     EDQGLFEISA AEMKSLHPLQ MGGLKVEMPM NLKVILYEKP HFLGHTKEFS EHIDSVPTFL
     KSDKDFHGIG SIRVIGGVWV AYEKEHFKGQ QFLLEEGDFE DSSACGALSG PIMSFRYLQA
     NFIESSITLF ESSHLESGKF IDITNQEISD LEEIGFGSET RSIHVKSGVW VAYHQKFFCG
     DQYILEKGKY KCFFDWGGSS NTILSIRPIQ LEPLGINEPT HLLKAFSKAG FQGECIDFVK
     ECADLTSFTP ASFKVLRGCW LLLYYQEDGF YHQCVLEEGL YVDLTSCGCP SARIRALQPI
     DYVFEEPSIS LFALEHCEGR ELHLEDAVNS VLNKDLHFYT QSVWIKSGLW IAYEGSNFLG
     RQILLTPKEI PNWTAFSGWK TIGSVRPMKQ PAVYIRIRNR AQDEYLTVTG NPADARTMSV
     CISPYSGKDT QIWHYCRGLF KSKASHTCLD VIGGRDTPGA KVALWTEHGQ LRQKWRMSRN
     GTISSYLSDE LVLDVKGGNY YDKTHVIVNQ PLEGEETQKW DIEIL
 
 
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