CRBB1_MOUSE
ID CRBB1_MOUSE Reviewed; 250 AA.
AC Q9WVJ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-crystallin B1;
DE AltName: Full=Beta-B1 crystallin;
DE Contains:
DE RecName: Full=Beta-crystallin B1B;
GN Name=Crybb1;
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 [MRNA].
RA Duncan M.K., Hejtmancik J.F., Piatigorsky J.;
RT "Beta-B1 crystallin: evidence for changes in gene regulation during
RT evolution.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Head;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
CC -!- SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure
CC of beta-crystallin oligomers seems to be stabilized through
CC interactions between the N-terminal arms.
CC -!- INTERACTION:
CC Q9WVJ5; P23928: Cryab; Xeno; NbExp=2; IntAct=EBI-8520354, EBI-916888;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- PTM: Specific cleavages in the N-terminal arm occur during lens
CC maturation and give rise to truncated forms, leading to impaired
CC oligomerization and protein insolubilization. The protease responsible
CC for this partial degradation could be calpain II.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; AF106853; AAD42048.1; -; mRNA.
DR EMBL; AK014012; BAB29113.1; -; mRNA.
DR EMBL; AK053869; BAC35565.1; -; mRNA.
DR CCDS; CCDS19537.1; -.
DR RefSeq; NP_001299822.1; NM_001312893.1.
DR RefSeq; NP_001299823.1; NM_001312894.1.
DR RefSeq; NP_001299824.1; NM_001312895.1.
DR RefSeq; NP_076184.1; NM_023695.3.
DR RefSeq; XP_006534818.1; XM_006534755.3.
DR RefSeq; XP_006534819.1; XM_006534756.2.
DR RefSeq; XP_006534820.1; XM_006534757.2.
DR AlphaFoldDB; Q9WVJ5; -.
DR SMR; Q9WVJ5; -.
DR BioGRID; 198913; 1.
DR IntAct; Q9WVJ5; 1.
DR MINT; Q9WVJ5; -.
DR STRING; 10090.ENSMUSP00000031286; -.
DR PhosphoSitePlus; Q9WVJ5; -.
DR MaxQB; Q9WVJ5; -.
DR PaxDb; Q9WVJ5; -.
DR PRIDE; Q9WVJ5; -.
DR ProteomicsDB; 283821; -.
DR Antibodypedia; 24283; 171 antibodies from 26 providers.
DR DNASU; 12960; -.
DR Ensembl; ENSMUST00000031286; ENSMUSP00000031286; ENSMUSG00000029343.
DR Ensembl; ENSMUST00000112375; ENSMUSP00000107994; ENSMUSG00000029343.
DR GeneID; 12960; -.
DR KEGG; mmu:12960; -.
DR UCSC; uc008ysv.1; mouse.
DR CTD; 1414; -.
DR MGI; MGI:104992; Crybb1.
DR VEuPathDB; HostDB:ENSMUSG00000029343; -.
DR eggNOG; ENOG502QTJT; Eukaryota.
DR GeneTree; ENSGT00940000160516; -.
DR InParanoid; Q9WVJ5; -.
DR OMA; AQEHKIC; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; Q9WVJ5; -.
DR TreeFam; TF331401; -.
DR BioGRID-ORCS; 12960; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Crybb1; mouse.
DR PRO; PR:Q9WVJ5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WVJ5; protein.
DR Bgee; ENSMUSG00000029343; Expressed in lens of camera-type eye and 96 other tissues.
DR ExpressionAtlas; Q9WVJ5; baseline and differential.
DR Genevisible; Q9WVJ5; MM.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:MGI.
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 InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033059; CRYBB1.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF12; PTHR11818:SF12; 1.
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 Acetylation; Eye lens protein; Methylation; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53674"
FT CHAIN 2..250
FT /note="Beta-crystallin B1"
FT /id="PRO_0000006337"
FT CHAIN 12..250
FT /note="Beta-crystallin B1B"
FT /id="PRO_0000006338"
FT DOMAIN 57..96
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 97..141
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 147..188
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 189..231
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..56
FT /note="N-terminal arm"
FT REGION 142..146
FT /note="Connecting peptide"
FT REGION 233..250
FT /note="C-terminal arm"
FT COMPBIAS 28..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P53674"
SQ SEQUENCE 250 AA; 28003 MW; CCF26E7D2F6B92EF CRC64;
MSQAAKASAT TAVNPGPDGK GKGAPSTGPA PAPGPTPVPA SVPRPAAKVG DLPPGSYRLI
VFEQENFQGR RVEFSGECLN LGDRGFDRVR SLIVVSGPWV AFEQSAFRGE MFVLEKGEYP
RWDTWTSSYR SDRLMSFRPI RMDSQEHKIC LFEGANFKGN TMEIQEDDVP SLWVYGFCDR
VGSITVSGGT WVGYQYPGYR GYQYLLEPGD FRHWNEWGAF QPQMQAVRRL RDRQWHQEGC
FPVLTAEPPK
