CRO_RANTE
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 03-AUG-2022, entry version 93.
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 PRIDE; P02532; -.
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 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