Reviewed, UniProtKB/Swiss-Prot P02532 (CRO_RANTE)

Names and origin

Protein names	Recommended name:     Rho crystallin
Organism	Rana temporaria (European common frog)
Taxonomic identifier	8407 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Rana

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Subunit structure	Monomer.
Sequence similarities	Belongs to the aldo/keto reductase family.
Caution	Was originally called epsilon crystallin.

Ontologies

Keywords
Cellular component	Eye lens protein
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: InterPro
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: InterPro structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 324	323	Rho crystallin		PRO_0000124614
Regions
	Nucleotide binding	218 – 281	64	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P02532-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 19D72B345982869F	FASTA	324	37,015
	10 20 30 40 50 60 MTLTKETRVT LNDGNMMPIL GLGTYASPHV PKSLAEEAVK IAIDVGYRHI DCAFITGNEM 70 80 90 100 110 120 HIGNGIRSKI SDGTVKREDI FYTGKLWCTY FSPEMVRKGL ERSLRDVGMD YLDLFLMHWP 130 140 150 160 170 180 VSLKPSGASD PSDKDKPFIY DNVDLCATWE ALEARKDAGL VRSLGVSNFN RRQLERILNK 190 200 210 220 230 240 PGLKYKPVCN QVECHVYLNQ NKLHSYCKSK DIVLVTYSVL GSHRDRNWVD LSLPVLLDDP 250 260 270 280 290 300 ILNKVAAKYN RTSAEIAMRF ILQKGIVVLA KSFTPARIKQ NLGVFEFELK PEDMKSLESL 310 320 DRNLHYGPFR EVKQHPEYPF HDEY

References

[1]	"Rho-crystallins from frog eye lens: structure and expression." Dolgilevich S.M., Mikaelian A.S., Kniazeva M.V., Snegovaia I.Y., Simirskii V.N., Aleinikova K.S., Gause G.G. Jr. Dokl. Akad. Nauk 335:373-377(1994) [PubMed: 8186748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[2]	"A novel type of crystallin in the frog eye lens. 35-kDa polypeptide is not homologous to any of the major classes of lens crystallins." Tomarev S.I., Zinovieva R.D., Dolgilevich S.M., Luchin S.V., Krayev A.S., Skryabin K.G., Gause G.G. Jr. FEBS Lett. 171:297-302(1984) [PubMed: 6609843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-324. Tissue: Lens.

Cross-references

Sequence databases

EMBLGenBankDDBJ

S70451 mRNA. Translation: AAB30820.1.
X00659 mRNA. Translation: CAA25277.1. Sequence problems.

PIR

CYFGE. A02938.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AR4	model	-	A	1-324	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P02532.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CRO_RANTE

Accession

Primary (citable) accession number: P02532

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	March 24, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)