CRO_LITCT
ID CRO_LITCT Reviewed; 324 AA.
AC P17264;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Rho crystallin;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=7575513; DOI=10.1006/bbrc.1995.2396;
RA Lu S.F., Pan F.M., Chiou S.H.;
RT "Sequence analysis of frog rho-crystallin by cDNA cloning and sequencing: a
RT member of the aldo-keto reductase family.";
RL Biochem. Biophys. Res. Commun. 214:1079-1088(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-324, AND ACETYLATION AT THR-2.
RC TISSUE=Lens;
RX PubMed=2190986; DOI=10.1016/s0021-9258(19)38759-9;
RA Fujii Y., Watanabe K., Hayashi H., Urade Y., Kuramitsu S., Kagamiyama H.,
RA Hayaishi O.;
RT "Purification and characterization of rho-crystallin from Japanese common
RT bullfrog lens.";
RL J. Biol. Chem. 265:9914-9923(1990).
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; X87724; CAA61023.1; -; mRNA.
DR PIR; JC4280; JC4280.
DR AlphaFoldDB; P17264; -.
DR SMR; P17264; -.
DR iPTMnet; P17264; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR CDD; cd19108; AKR_AKR1C1-35; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044482; AKR1C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Eye lens protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2190986"
FT CHAIN 2..324
FT /note="Rho crystallin"
FT /id="PRO_0000124613"
FT BINDING 218..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:2190986"
FT CONFLICT 76
FT /note="K -> E (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="R -> C (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="S -> A (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> A (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="P -> A (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="T -> S (in Ref. 1; CAA61023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36965 MW; 61FFCDACF29894BE CRC64;
MTLTKETRVT LNDGNMMPIL GLGTYAAPDV PKSLAEEAVK TAIDVGYRHI DCAFITGNEM
HIGNGIRSKI SDGTVKREDI FYTGKLWCTY FSPDMVRKGL ERSLRDVGMD YLDLFLMHWP
VSLKPSGASD PSDKDKPFIY DNVDLCATWE ALEARKDAGL VRSLGVSNFN RRQLERILNK
PGLKYKPVCN QVECHVYLNQ NKLHSYCKSK DIVLVTYSVL GSHRDRNWVD LSLPVLLDDP
ILNKIAAKYN RTSAEVAMRF ILQKGIVVLA KSFTPARIKQ NLGVFEFELK PEDMKTLESL
DRNLHYGPFR EVKQHPEYPF HDEY
