P02775 (CXCL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet basic protein
Short name=PBP

Alternative name(s):
C-X-C motif chemokine 7
Leukocyte-derived growth factor
Short name=LDGF
Macrophage-derived growth factor
Short name=MDGF
Small-inducible cytokine B7

Cleaved into the following 10 chains:

1. Connective tissue-activating peptide III
   Short name=CTAP-III
   Alternative name(s):
   LA-PF4
   Low-affinity platelet factor IV
2. TC-2
3. Connective tissue-activating peptide III(1-81)
   Short name=CTAP-III(1-81)
4. Beta-thromboglobulin
   Short name=Beta-TG
5. Neutrophil-activating peptide 2(74)
   Short name=NAP-2(74)
6. Neutrophil-activating peptide 2(73)
   Short name=NAP-2(73)
7. Neutrophil-activating peptide 2
   Short name=NAP-2
8. TC-1
9. Neutrophil-activating peptide 2(1-66)
   Short name=NAP-2(1-66)
10. Neutrophil-activating peptide 2(1-63)
    Short name=NAP-2(1-63)

Gene names

Name:	PPBP
Synonyms:	CTAP3, CXCL7, SCYB7, TGB1, THBGB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	128 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)

Function	LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation. Ref.11 Ref.15 Ref.18 Ref.21
Subunit structure	Beta-thromboglobulin is a homotetramer.
Subcellular location	Secreted.
Post-translational modification	Proteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)). Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor. NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils. NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets.
Sequence similarities	Belongs to the intercrine alpha (chemokine CxC) family.

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Cytokine Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW neutrophil chemotaxis Inferred from electronic annotation. Source: InterPro neutrophil degranulation Inferred from electronic annotation. Source: InterPro platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: UniProtKB-KW platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	glucose transmembrane transporter activity Traceable author statement PubMed 4005226. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.9 Ref.10

Chain

35 – 128

94

Platelet basic protein

PRO_0000005088

Chain

44 – 128

85

Connective tissue-activating peptide III

PRO_0000005089

Chain

44 – 126

83

TC-2

PRO_0000005090

Chain

44 – 124

81

Connective tissue-activating peptide III(1-81)

PRO_0000041949

Chain

48 – 128

81

Beta-thromboglobulin

PRO_0000005091

Chain

55 – 128

74

Neutrophil-activating peptide 2(74)

PRO_0000005092

Chain

56 – 128

73

Neutrophil-activating peptide 2(73)

PRO_0000005093

Chain

59 – 128

70

Neutrophil-activating peptide 2

PRO_0000005094

Chain

59 – 126

68

TC-1

PRO_0000005095

Chain

59 – 124

66

Neutrophil-activating peptide 2(1-66)

PRO_0000005096

Chain

59 – 121

63

Neutrophil-activating peptide 2(1-63)

PRO_0000041950

Amino acid modifications

Disulfide bond

63 ↔ 89

Disulfide bond

65 ↔ 105

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

128

Helix Strand Turn

Details...

Beta strand

50 – 54

5

Helix

58 – 60

3

Helix

74 – 76

3

Beta strand

77 – 83

7

Beta strand

89 – 91

3

Beta strand

93 – 98

6

Beta strand

103 – 106

4

Helix

111 – 122

12

Sequences

	Sequence		Length	Mass (Da)
	P02775 [UniParc]. Last modified November 1, 1991. Version 3. Checksum: BEAB7B75916723D9	FASTA	128	13,894
	10 20 30 40 50 60 MSLRLDTTPS CNSARPLHAL QVLLLLSLLL TALASSTKGQ TKRNLAKGKE ESLDSDLYAE 70 80 90 100 110 120 LRCMCIKTTS GIHPKNIQSL EVIGKGTHCN QVEVIATLKD GRKICLDPDA PRIKKIVQKK LAGDESAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library." Wenger R.H., Wicki A.N., Walz A., Kieffer N., Clemetson K.J. Blood 73:1498-1503(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Platelet.
[2]	"Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4." Majumdar S., Gonder D., Koutsis B., Poncz M. J. Biol. Chem. 266:5785-5789(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Localization of distal regulatory domains in the megakaryocyte-specific platelet basic protein/platelet factor 4 gene locus." Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M., Poncz M., McKenzie S.E., Reilly M.P. Blood 98:610-617(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Leukocyte.
[9]	"Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin." Holt J.C., Harris M.E., Holt A.M., Lange E., Henschen A., Niewiarowski S. Biochemistry 25:1988-1996(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-53.
[10]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-49.
[11]	"Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines." Krijgsveld J., Zaat S.A., Meeldijk J., van Veelen P.A., Fang G., Poolman B., Brandt E., Ehlert J.E., Kuijpers A.J., Engbers G.H., Feijen J., Dankert J. J. Biol. Chem. 275:20374-20381(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-126, IDENTIFICATION OF TC-1 AND TC-2, FUNCTION.
[12]	"Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor." Castor C.W., Miller J.W., Walz D.A. Proc. Natl. Acad. Sci. U.S.A. 80:765-769(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-66 AND 125-128.
[13]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-62. Tissue: Platelet.
[14]	"Complete covalent structure of human beta-thromboglobulin." Begg G.S., Pepper D.S., Chesterman C.N., Morgan F.J. Biochemistry 17:1739-1744(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-126.
[15]	"Thrombin-activated human platelets release two NAP-2 variants that stimulate polymorphonuclear leukocytes." Piccardoni P., Evangelista V., Piccoli A., de Gaetano G., Walz A., Cerletti C. Thromb. Haemost. 76:780-785(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 55-128, IDENTIFICATION OF NAP-2(73) AND NAP-2(74), FUNCTION. Tissue: Platelet.
[16]	"Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets." Castor C.W., Walz D.A., Ragsdale C.G., Hossler P.A., Smith E.M., Bignall M.C., Aaron B.P., Mountjoy K. Biochem. Biophys. Res. Commun. 163:1071-1078(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-68.
[17]	"A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils." Walz A., Baggiolini M. Biochem. Biophys. Res. Commun. 159:969-975(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-126.
[18]	"Limited and defined truncation at the C-terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2). Comparison of native and recombinant NAP-2 variants." Ehlert J.E., Petersen F., Kubbutat M.H., Gerdes J., Flad H.D., Brandt E. J. Biol. Chem. 270:6338-6344(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-124, IDENTIFICATION OF NAP-2(1-66), FUNCTION. Tissue: Peripheral blood monocyte.
[19]	"Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases." Walz A., Baggiolini M. J. Exp. Med. 171:449-454(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-67.
[20]	"Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide." Clark-Lewis I., Mose B., Walz A., Baggiolini M., Scott G.J., Aebersold R. Biochemistry 30:3128-3135(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SYNTHESIS OF 59-126.
[21]	"Novel C-terminally truncated isoforms of the CXC chemokine beta-thromboglobulin and their impact on neutrophil functions." Ehlert J.E., Gerdes J., Flad H.-D., Brandt E. J. Immunol. 161:4975-4982(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF CTAP-III(1-81) AND NAP-2(1-63), FUNCTION, PROTEOLYTIC PROCESSING OF C-TERMINAL.
[22]	"Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2)." Kungl A.J., Machius M., Huber R., Schwer C., Lam C., Aschauer H., Ehn G., Lindley I.J.D., Auer M. FEBS Lett. 347:300-303(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 59-128.
[23]	"The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution." Malkowski M.G., Wu J.Y., Lazar J.B., Johnson P.H., Edwards B.F.P. J. Biol. Chem. 270:7077-7087(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-128.
+	Additional computationally mapped references.

Web resources

Wikipedia

CXCL7 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M54995 mRNA. Translation: AAA62836.1.
AF349466 Genomic DNA. Translation: AAK29642.1.
CR456805 mRNA. Translation: CAG33086.1.
AC097709 Genomic DNA. Translation: AAY41004.1.
AK312166 mRNA. Translation: BAG35100.1.
CH471057 Genomic DNA. Translation: EAX05695.1.
BC028217 mRNA. Translation: AAH28217.1.

IPI

IPI00022445.

PIR

TGHU. A39546.

RefSeq

NP_002695.1. NM_002704.3.

UniGene

Hs.2164.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F9P	X-ray	1.93	A	44-128	[»]
1NAP	X-ray	1.90	A/B/C/D	59-128	[»]
1TVX	X-ray	1.75	A/B/C/D	54-128	[»]

ProteinModelPortal

P02775.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5913N.

IntAct

P02775. 12 interactions.

MINT

MINT-1393871.

STRING

9606.ENSP00000296028.

PTM databases

PhosphoSite

P02775.

Polymorphism databases

DMDM

129874.

2D gel databases

SWISS-2DPAGE

P02775.

Proteomic databases

PaxDb

P02775.

PeptideAtlas

P02775.

PRIDE

P02775.

Protocols and materials databases

DNASU

5473.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296028; ENSP00000296028; ENSG00000163736.

GeneID

5473.

KEGG

hsa:5473.

UCSC

uc003hhj.3. human.

Organism-specific databases

CTD

5473.

GeneCards

GC04M074841.

H-InvDB

HIX0031528.

HGNC

HGNC:9240. PPBP.

HPA

CAB017624.
HPA008354.

MIM

121010. gene.

neXtProt

NX_P02775.

PharmGKB

PA33561.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39945.

HOGENOM

HOG000220915.

HOVERGEN

HBG107789.

InParanoid

P02775.

KO

K10029.

OMA

LYAELRC.

OrthoDB

EOG4Z8XZ6.

PhylomeDB

P02775.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02775.

Bgee

P02775.

CleanEx

HS_PPBP.

Genevestigator

P02775.

GermOnline

ENSG00000163736. Homo sapiens.

Family and domain databases

InterPro

IPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
IPR027223. PPBP.
[Graphical view]

PANTHER

PTHR10179. PTHR10179. 1 hit.
PTHR10179:SF14. PTHR10179:SF14. 1 hit.

Pfam

PF00048. IL8. 1 hit.
[Graphical view]

PRINTS

PR00437. SMALLCYTKCXC.

SMART

SM00199. SCY. 1 hit.
[Graphical view]

SUPFAM

SSF54117. Chemokine_IL8. 1 hit.

PROSITE

PS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02775.

GenomeRNAi

5473.

NextBio

21188.

PMAP-CutDB

P02775.

SOURCE

Search...

Entry information

Entry name

CXCL7_HUMAN

Accession

Primary (citable) accession number: P02775
Secondary accession number(s): B2R5F3, Q6IBJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.