ID CRO_RANTE Reviewed; 324 AA. AC P02532; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 104. DE RecName: Full=Rho crystallin; OS Rana temporaria (European common frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana. OX NCBI_TaxID=8407; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lens; RX PubMed=8186748; RA Dolgilevich S.M., Mikaelian A.S., Kniazeva M.V., Snegovaia I.Y., RA Simirskii V.N., Aleinikova K.S., Gause G.G. Jr.; RT "Rho-crystallins from frog eye lens: structure and expression."; RL Dokl. Akad. Nauk 335:373-377(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-324. RC TISSUE=Lens; RX PubMed=6609843; DOI=10.1016/0014-5793(84)80508-6; RA Tomarev S.I., Zinovieva R.D., Dolgilevich S.M., Luchin S.V., Krayev A.S., RA Skryabin K.G., Gause G.G. Jr.; RT "A novel type of crystallin in the frog eye lens. 35-kDa polypeptide is not RT homologous to any of the major classes of lens crystallins."; RL FEBS Lett. 171:297-302(1984). CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}. CC -!- CAUTION: Was originally called epsilon crystallin. {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; S70451; AAB30820.1; -; mRNA. DR EMBL; X00659; CAA25277.1; ALT_SEQ; mRNA. DR PIR; A02938; CYFGE. DR AlphaFoldDB; P02532; -. DR SMR; P02532; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR CDD; cd19108; AKR_AKR1C1-35; 1. DR FunFam; 3.20.20.100:FF:000003; Aldo-keto reductase family 1 member C3; 1. DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1. DR InterPro; IPR020471; AKR. DR InterPro; IPR044482; AKR1C. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR036812; NAD(P)_OxRdtase_dom_sf. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 2: Evidence at transcript level; KW Acetylation; Eye lens protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..324 FT /note="Rho crystallin" FT /id="PRO_0000124614" 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:0000250" SQ SEQUENCE 324 AA; 37015 MW; 19D72B345982869F CRC64; MTLTKETRVT LNDGNMMPIL GLGTYASPHV PKSLAEEAVK IAIDVGYRHI DCAFITGNEM HIGNGIRSKI SDGTVKREDI FYTGKLWCTY FSPEMVRKGL ERSLRDVGMD YLDLFLMHWP VSLKPSGASD PSDKDKPFIY DNVDLCATWE ALEARKDAGL VRSLGVSNFN RRQLERILNK PGLKYKPVCN QVECHVYLNQ NKLHSYCKSK DIVLVTYSVL GSHRDRNWVD LSLPVLLDDP ILNKVAAKYN RTSAEIAMRF ILQKGIVVLA KSFTPARIKQ NLGVFEFELK PEDMKSLESL DRNLHYGPFR EVKQHPEYPF HDEY //