CRBB2_CANLF
ID CRBB2_CANLF Reviewed; 205 AA.
AC Q2LEC2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Beta-crystallin B2;
DE AltName: Full=Beta-B2 crystallin;
DE AltName: Full=Beta-crystallin Bp;
GN Name=CRYBB2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Wistow G.;
RL Submitted (DEC-2005) 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 -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ324463; ABC59315.1; -; mRNA.
DR RefSeq; NP_001041578.1; NM_001048113.1.
DR AlphaFoldDB; Q2LEC2; -.
DR SMR; Q2LEC2; -.
DR STRING; 9612.ENSCAFP00000017026; -.
DR PaxDb; Q2LEC2; -.
DR Ensembl; ENSCAFT00030048286; ENSCAFP00030042249; ENSCAFG00030026106.
DR Ensembl; ENSCAFT00040046977; ENSCAFP00040041009; ENSCAFG00040025194.
DR Ensembl; ENSCAFT00845049384; ENSCAFP00845038748; ENSCAFG00845027963.
DR GeneID; 486326; -.
DR KEGG; cfa:486326; -.
DR CTD; 1415; -.
DR VEuPathDB; HostDB:ENSCAFG00845027963; -.
DR eggNOG; ENOG502QVM6; Eukaryota.
DR GeneTree; ENSGT00940000160048; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; Q2LEC2; -.
DR OMA; TWVAYQY; -.
DR OrthoDB; 1237607at2759; -.
DR TreeFam; TF331401; -.
DR Proteomes; UP000002254; Chromosome 26.
DR Bgee; ENSCAFG00000023827; Expressed in tongue and 3 other tissues.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IPR033058; CRYBB2.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF11; PTHR11818:SF11; 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; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02522"
FT CHAIN 2..205
FT /note="Beta-crystallin B2"
FT /id="PRO_0000289593"
FT DOMAIN 17..56
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 57..101
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 107..148
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 149..191
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..16
FT /note="N-terminal arm"
FT REGION 102..106
FT /note="Connecting peptide"
FT REGION 193..205
FT /note="C-terminal arm"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02522"
SQ SEQUENCE 205 AA; 23333 MW; 35020BEFB7D068F9 CRC64;
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELSGPCPN LKETGVEKAG SVLVQAGPWV
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK
KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSGDFGAP
HPQVQSVRRI RDMQWHQRGA FHPSN