ID   CRBB1_PIG               Reviewed;         249 AA.
AC   Q007T1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Beta-crystallin B1;
DE   AltName: Full=Beta-B1 crystallin;
GN   Name=CRYBB1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Crystallins are the dominant structural components of the
CC       vertebrate eye lens. {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; DQ915497; ABJ09402.1; -; mRNA.
DR   RefSeq; NP_001072149.1; NM_001078681.1.
DR   AlphaFoldDB; Q007T1; -.
DR   SMR; Q007T1; -.
DR   STRING; 9823.ENSSSCP00000010635; -.
DR   PaxDb; Q007T1; -.
DR   PeptideAtlas; Q007T1; -.
DR   PRIDE; Q007T1; -.
DR   Ensembl; ENSSSCT00000010920; ENSSSCP00000010635; ENSSSCG00000009964.
DR   Ensembl; ENSSSCT00005042015; ENSSSCP00005025702; ENSSSCG00005026533.
DR   Ensembl; ENSSSCT00015027140; ENSSSCP00015010622; ENSSSCG00015020430.
DR   Ensembl; ENSSSCT00025060751; ENSSSCP00025025774; ENSSSCG00025044723.
DR   Ensembl; ENSSSCT00030050507; ENSSSCP00030022960; ENSSSCG00030036323.
DR   Ensembl; ENSSSCT00035044650; ENSSSCP00035017864; ENSSSCG00035033700.
DR   Ensembl; ENSSSCT00040021823; ENSSSCP00040009111; ENSSSCG00040016225.
DR   Ensembl; ENSSSCT00045027577; ENSSSCP00045019073; ENSSSCG00045016207.
DR   Ensembl; ENSSSCT00050008713; ENSSSCP00050003740; ENSSSCG00050006375.
DR   Ensembl; ENSSSCT00055044482; ENSSSCP00055035448; ENSSSCG00055022632.
DR   Ensembl; ENSSSCT00060076312; ENSSSCP00060032982; ENSSSCG00060056006.
DR   Ensembl; ENSSSCT00065021169; ENSSSCP00065008558; ENSSSCG00065015968.
DR   Ensembl; ENSSSCT00070001689; ENSSSCP00070001431; ENSSSCG00070000876.
DR   GeneID; 780429; -.
DR   KEGG; ssc:780429; -.
DR   CTD; 1414; -.
DR   VGNC; VGNC:87015; CRYBB1.
DR   eggNOG; ENOG502QTJT; Eukaryota.
DR   GeneTree; ENSGT00940000160516; -.
DR   HOGENOM; CLU_081883_0_1_1; -.
DR   InParanoid; Q007T1; -.
DR   OMA; AQEHKIC; -.
DR   OrthoDB; 1237607at2759; -.
DR   TreeFam; TF331401; -.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Proteomes; UP000314985; Chromosome 14.
DR   Bgee; ENSSSCG00000009964; Expressed in oocyte and 16 other tissues.
DR   Genevisible; Q007T1; SS.
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   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   2: Evidence at transcript 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..249
FT                   /note="Beta-crystallin B1"
FT                   /id="PRO_0000289660"
FT   DOMAIN          56..95
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          96..140
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          146..187
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          188..230
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..55
FT                   /note="N-terminal arm"
FT   REGION          141..145
FT                   /note="Connecting peptide"
FT   REGION          232..249
FT                   /note="C-terminal arm"
FT   COMPBIAS        21..39
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   249 AA;  27912 MW;  EF5B462C1187FA36 CRC64;
     MSQPAVKASA TAAVNPGPDG KGKGAPPPGP APGSGPAQAP AQPMPAAKGD LPPGSYKLVV
     FEQENFQGRR VEFSGECLNL GDRGFDRVRS IIVTSGPWVA FEQSNFRGEM FILEKGEYPR
     WDTWSSSYRS DRLMSFRPIR MDAQEHKLCL FEGANFKGNT MEIQEDDVPS LWVYGFCDRV
     GSVRVSSGTW VGYQYPGYRG YQYLLEPGDF RHWNDWGAFQ PQMQAVRRLR DRQWHREGCF
     PVLAAEPPK