P17264 (CRO_RANCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Rho crystallin
Organism	Rana catesbeiana (American bullfrog) (Lithobates catesbeiana)
Taxonomic identifier	8400 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Raninae › Rana › Aquarana

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 protein level

General annotation (Comments)

Subunit structure	Monomer.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Molecular function	Eye lens protein
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
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 Ref.2

Chain

2 – 324

323

Rho crystallin

PRO_0000124613

Regions

Nucleotide binding

218 – 281

64

NADP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.2

Experimental info

Sequence conflict

76

1

K → E in CAA61023. Ref.1

Sequence conflict

155

1

R → C in CAA61023. Ref.1

Sequence conflict

205

1

S → A in CAA61023. Ref.1

Sequence conflict

216

1

T → A in CAA61023. Ref.1

Sequence conflict

234

1

P → A in CAA61023. Ref.1

Sequence conflict

252

1

T → S in CAA61023. Ref.1

Secondary structure

1

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324

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

7 – 9

3

Beta strand

15 – 22

8

Helix

33 – 43

11

Beta strand

48 – 50

3

Turn

53 – 56

4

Helix

58 – 70

13

Helix

76 – 78

3

Beta strand

80 – 85

6

Helix

87 – 89

3

Turn

92 – 94

3

Helix

95 – 106

12

Beta strand

111 – 117

7

Beta strand

124 – 129

6

Helix

144 – 156

13

Beta strand

159 – 167

9

Helix

170 – 177

8

Beta strand

187 – 192

6

Helix

200 – 209

10

Beta strand

212 – 217

6

Turn

225 – 227

3

Helix

235 – 237

3

Helix

239 – 247

9

Helix

252 – 261

10

Turn

262 – 264

3

Beta strand

266 – 269

4

Helix

274 – 280

7

Helix

281 – 285

5

Helix

290 – 298

9

Helix

309 – 311

3

Sequences

	Sequence		Length	Mass (Da)
	P17264 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 61FFCDACF29894BE	FASTA	324	36,965
	10 20 30 40 50 60 MTLTKETRVT LNDGNMMPIL GLGTYAAPDV PKSLAEEAVK TAIDVGYRHI DCAFITGNEM 70 80 90 100 110 120 HIGNGIRSKI SDGTVKREDI FYTGKLWCTY FSPDMVRKGL 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 ILNKIAAKYN RTSAEVAMRF ILQKGIVVLA KSFTPARIKQ NLGVFEFELK PEDMKTLESL 310 320 DRNLHYGPFR EVKQHPEYPF HDEY

References

[1]	"Sequence analysis of frog rho-crystallin by cDNA cloning and sequencing: a member of the aldo-keto reductase family." Lu S.F., Pan F.M., Chiou S.H. Biochem. Biophys. Res. Commun. 214:1079-1088(1995) [PubMed: 7575513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[2]	"Purification and characterization of rho-crystallin from Japanese common bullfrog lens." Fujii Y., Watanabe K., Hayashi H., Urade Y., Kuramitsu S., Kagamiyama H., Hayaishi O. J. Biol. Chem. 265:9914-9923(1990) [PubMed: 2190986] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-324. Tissue: Lens.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X87724 mRNA. Translation: CAA61023.1.

PIR

JC4280.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P17264.

SMR

P17264. Positions 5-324.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG000020.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[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]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

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_RANCA

Accession

Primary (citable) accession number: P17264

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 28, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program