P02699 (OPSD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rhodopsin

Gene names

Name:

RHO

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal By similarity. Ref.26 Ref.27
Subunit structure	Homodimer. Ref.31
Subcellular location	Membrane; Multi-pass membrane protein. Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia By similarity.
Tissue specificity	Rod shaped photoreceptor cells which mediates vision in dim light.
Post-translational modification	Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. Ref.10 Ref.18 Ref.19 Contains one covalently linked retinal chromophore.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Biophysicochemical properties	Absorption: Abs(max)=495 nm

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore Metal-binding Zinc
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Acetylation Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor inner segment membrane Inferred from sequence or structural similarity. Source: UniProtKB photoreceptor outer segment membrane Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Rhodopsin

PRO_0000197653

Regions

Topological domain

1 – 36

36

Extracellular

Transmembrane

37 – 63

27

Helical; Name=1

Topological domain

64 – 73

10

Cytoplasmic

Transmembrane

74 – 96

23

Helical; Name=2

Topological domain

97 – 110

14

Extracellular

Transmembrane

111 – 133

23

Helical; Name=3

Topological domain

134 – 152

19

Cytoplasmic

Transmembrane

153 – 173

21

Helical; Name=4

Topological domain

174 – 202

29

Extracellular

Transmembrane

203 – 224

22

Helical; Name=5

Topological domain

225 – 249

25

Cytoplasmic

Transmembrane

250 – 274

25

Helical; Name=6

Topological domain

275 – 286

12

Extracellular

Transmembrane

287 – 308

22

Helical; Name=7

Topological domain

309 – 348

40

Cytoplasmic

Region

113 – 125

13

Retinal chromophore binding

Region

207 – 212

6

Retinal chromophore binding

Motif

134 – 137

4

'Ionic lock' involved in activated form stabilization

Sites

Metal binding

201

1

Zinc

Metal binding

279

1

Zinc

Binding site

265

1

Retinal chromophore

Binding site

296

1

Retinal chromophore (covalent)

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Modified residue

296

1

N6-(retinylidene)lysine

Modified residue

334

1

Phosphoserine By similarity

Modified residue

335

1

Phosphothreonine Ref.18 Ref.19

Modified residue

336

1

Phosphothreonine Ref.18 Ref.19

Modified residue

338

1

Phosphoserine By similarity

Modified residue

340

1

Phosphothreonine Ref.18 Ref.19

Modified residue

342

1

Phosphothreonine Ref.18 Ref.19

Modified residue

343

1

Phosphoserine; by RK and GRK7 Ref.10 Ref.18 Ref.19

Lipidation

322

1

S-palmitoyl cysteine Ref.8 Ref.11 Ref.14

Lipidation

323

1

S-palmitoyl cysteine Ref.8 Ref.11 Ref.14

Glycosylation

2

1

N-linked (GlcNAc...) Ref.1 Ref.6 Ref.14

Glycosylation

15

1

N-linked (GlcNAc...) Ref.1 Ref.6 Ref.14

Disulfide bond

110 ↔ 187

Ref.9

Experimental info

Mutagenesis

2

1

N → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. Ref.29

Mutagenesis

15

1

N → D: Normal light absorption; when associated with C-2 and C-282. Ref.29

Mutagenesis

282

1

D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. Ref.29

Sequence conflict

281

1

S → F in AAA30675. Ref.3

Secondary structure

1

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348

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

10 – 13

4

Turn

23 – 25

3

Helix

29 – 31

3

Helix

34 – 64

31

Helix

71 – 89

19

Helix

91 – 100

10

Helix

106 – 139

34

Beta strand

143 – 145

3

Helix

150 – 168

19

Helix

170 – 172

3

Beta strand

178 – 181

4

Turn

182 – 185

4

Beta strand

186 – 189

4

Turn

196 – 199

4

Helix

200 – 210

11

Helix

213 – 225

13

Helix

246 – 254

9

Helix

256 – 277

22

Helix

285 – 295

11

Helix

296 – 299

4

Helix

301 – 309

9

Helix

311 – 321

11

Turn

322 – 324

3

Beta strand

338 – 342

5

Sequences

	Sequence		Length	Mass (Da)
	P02699 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 33FDA196803E81F3	FASTA	348	39,008
	10 20 30 40 50 60 MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML GFPINFLTLY 70 80 90 100 110 120 VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG 130 140 150 160 170 180 GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP 190 200 210 220 230 240 EGMQCSCGID YYTPHEETNN ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES 250 260 270 280 290 300 ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV 310 320 330 340 YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA

References

[1]	"Rhodopsin and bacteriorhodopsin: structure-function relationships." Ovchinnikov Y.A. FEBS Lett. 148:179-191(1982) [PubMed: 6759163] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin." Nathans J., Hogness D.S. Cell 34:807-814(1983) [PubMed: 6194890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Multiple opsin mRNA species in bovine retina." Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N. Brain Res. 387:251-260(1986) [PubMed: 2950966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
[4]	"Isolation and nucleotide sequence of a partial cDNA clone for bovine opsin." Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M., Tokunaga F. Biochem. Biophys. Res. Commun. 116:563-567(1983) [PubMed: 6228228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
[5]	"Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin." Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B., Galijatovic A., Chen N., Crouch R.K., Knapp D.R. Protein Sci. 7:758-764(1998) [PubMed: 9541408] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Retina.
[6]	"Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus." Fukuda M.N., Papermaster D.S., Hargrave P.A. J. Biol. Chem. 254:8201-8207(1979) [PubMed: 468821] [Abstract] Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
[7]	"Structural studies on membrane-bound bovine rhodopsin." Mullen E., Akhtar M. Biochem. J. 211:45-54(1983) [PubMed: 6870827] [Abstract] Cited for: RETINAL-BINDING SITE.
[8]	"Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated." Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S. FEBS Lett. 230:1-5(1988) [PubMed: 3350146] [Abstract] Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[9]	"Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187." Karnik S.S., Khorana H.G. J. Biol. Chem. 265:17520-17524(1990) [PubMed: 2145276] [Abstract] Cited for: DISULFIDE BOND.
[10]	"Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin." Brown N.G., Fowles C., Sharma R., Akhtar M. Eur. J. Biochem. 208:659-667(1992) [PubMed: 1396673] [Abstract] Cited for: PHOSPHORYLATION AT SER-343.
[11]	"Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry." Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R. J. Biol. Chem. 267:16889-16894(1992) [PubMed: 1512231] [Abstract] Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[12]	"Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops." Cai K., Langen R., Hubbell W.L., Khorana H.G. Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997) [PubMed: 9405601] [Abstract] Cited for: MUTAGENESIS.
[13]	"Crystal structure of rhodopsin: a G protein-coupled receptor." Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., Miyano M. Science 289:739-745(2000) [PubMed: 10926528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]	"Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)." Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E. Biochemistry 40:7761-7772(2001) [PubMed: 11425302] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, GLYCOSYLATION AT ASN-2 AND ASN-15.
[15]	"Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms." Yeagle P.L., Choi G., Albert A.D. Biochemistry 40:11932-11937(2001) [PubMed: 11570894] [Abstract] Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
[16]	"Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin." Choi G., Landin J., Galan J.F., Birge R.R., Albert A.D., Yeagle P.L. Biochemistry 41:7318-7324(2002) [PubMed: 12044163] [Abstract] Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
[17]	"Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography." Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y. Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002) [PubMed: 11972040] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[18]	"The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin." Kisselev O.G., McDowell J.H., Hargrave P.A. FEBS Lett. 564:307-311(2004) [PubMed: 15111114] [Abstract] Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
[19]	"Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions." Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A. J. Biol. Chem. 279:51203-51207(2004) [PubMed: 15351781] [Abstract] Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
[20]	"The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure." Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V. J. Mol. Biol. 342:571-583(2004) [PubMed: 15327956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[21]	"Structure of bovine rhodopsin in a trigonal crystal form." Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F. J. Mol. Biol. 343:1409-1438(2004) [PubMed: 15491621] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[22]	"Structure of the third cytoplasmic loop of bovine rhodopsin." Yeagle P.L., Alderfer J.L., Albert A.D. Biochemistry 34:14621-14625(1995) [PubMed: 7578070] [Abstract] Cited for: STRUCTURE BY NMR OF 231-252.
[23]	"Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin." Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G., Alderfer J.L., Albert A.D. J. Pept. Res. 55:455-465(2000) [PubMed: 10888202] [Abstract] Cited for: STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
[24]	"Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin." Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D. Mol. Vis. 6:125-131(2000) [PubMed: 10930473] [Abstract] Cited for: STRUCTURE BY NMR OF 291-315.
[25]	"Crystallographic analysis of primary visual photochemistry." Nakamichi H., Okada T. Angew. Chem. Int. Ed. 45:4270-4273(2006) [PubMed: 16586416] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE.
[26]	"Local peptide movement in the photoreaction intermediate of rhodopsin." Nakamichi H., Okada T. Proc. Natl. Acad. Sci. U.S.A. 103:12729-12734(2006) [PubMed: 16908857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
[27]	"Crystal structure of a photoactivated deprotonated intermediate of rhodopsin." Salom D., Lodowski D.T., Stenkamp R.E., Le Trong I., Golczak M., Jastrzebska B., Harris T., Ballesteros J.A., Palczewski K. Proc. Natl. Acad. Sci. U.S.A. 103:16123-16128(2006) [PubMed: 17060607] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
[28]	"Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography." Nakamichi H., Buss V., Okada T. Biophys. J. 92:L106-L108(2007) [PubMed: 17449675] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS IN COMPLEX WITH RETINAL CHROMOPHORE.
[29]	"Crystal structure of a thermally stable rhodopsin mutant." Standfuss J., Xie G., Edwards P.C., Burghammer M., Oprian D.D., Schertler G.F. J. Mol. Biol. 372:1179-1188(2007) [PubMed: 17825322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, MUTAGENESIS OF ASN-2; ASN-15 AND ASP-282.
[30]	"Alternative models for two crystal structures of bovine rhodopsin." Stenkamp R.E. Acta Crystallogr. D 64:902-904(2008) [PubMed: 18645239] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[31]	"Crystal structure of the ligand-free G-protein-coupled receptor opsin." Park J.H., Scheerer P., Hofmann K.P., Choe H.-W., Ernst O.P. Nature 454:183-187(2008) [PubMed: 18563085] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DIMERIZATION.
[32]	"Crystal structure of opsin in its G-protein-interacting conformation." Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.-W., Hofmann K.P., Ernst O.P. Nature 455:497-502(2008) [PubMed: 18818650] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), ACTIVATION MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K00506 , K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.

IPI

IPI00712873.

PIR

OOBO. A90840.

RefSeq

NP_001014890.1. NM_001014890.1.

UniGene

Bt.12753.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOJ	model	-	A	1-348	[»]
1BOK	model	-	A	1-348	[»]
1EDS	NMR	-	A	93-123	[»]
1EDV	NMR	-	A	172-205	[»]
1EDW	NMR	-	A	268-293	[»]
1EDX	NMR	-	A	1-40	[»]
1F88	X-ray	2.80	A/B	1-348	[»]
1FDF	NMR	-	A	291-315	[»]
1GZM	X-ray	2.65	A/B	1-348	[»]
1HZX	X-ray	2.80	A/B	1-348	[»]
1JFP	NMR	-	A	1-348	[»]
1L9H	X-ray	2.60	A/B	1-348	[»]
1LN6	NMR	-	A	1-348	[»]
1N3M	model	-	A/B/C/D/E/F	1-348	[»]
1NZS	NMR	-	A	330-348	[»]
1OV0	model	-	A	1-348	[»]
1OV1	model	-	A	1-348	[»]
1U19	X-ray	2.20	A/B	1-348	[»]
1VQX	NMR	-	A	330-348	[»]
2G87	X-ray	2.60	A/B	1-348	[»]
2HPY	X-ray	2.80	A/B	1-348	[»]
2I35	X-ray	3.80	A	1-348	[»]
2I36	X-ray	4.10	A/B/C	1-348	[»]
2I37	X-ray	4.15	A/B/C	1-348	[»]
2IQK	model	-	A	1-348	[»]
2J4Y	X-ray	3.40	A/B	3-348	[»]
2PED	X-ray	2.95	A/B	1-348	[»]
2X72	X-ray	3.00	A	3-348	[»]
3C9L	X-ray	2.65	A	1-348	[»]
3C9M	X-ray	3.40	A	3-348	[»]
3CAP	X-ray	2.90	A/B	1-348	[»]
3DQB	X-ray	3.20	A	1-348	[»]
3OAX	X-ray	2.60	A/B	1-348	[»]
3PQR	X-ray	2.85	A	1-348	[»]
3PXO	X-ray	3.00	A	1-348	[»]

ProteinModelPortal

P02699.

SMR

P02699. Positions 1-348.

DisProt

DP00271.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29225N.

STRING

P02699.

Protein family/group databases

GPCRDB

Search...

PTM databases

GlycoSuiteDB

P02699.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.

GeneID

509933.

KEGG

bta:509933.

Organism-specific databases

CTD

6010.

Phylogenomic databases

eggNOG

maNOG05931.

GeneTree

ENSGT00550000074069.

HOVERGEN

HBG107442.

InParanoid

P02699.

OrthoDB

EOG4P5K9D.

PhylomeDB

P02699.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
IPR001760. Opsin.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]

KO

K04250.

Pfam

PF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

OPSD_BOVIN

Accession

Primary (citable) accession number: P02699

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 16, 2011
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program