P07108 (ACBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-CoA-binding protein
Short name=ACBP

Alternative name(s):
Diazepam-binding inhibitor
Short name=DBI
Endozepine
Short name=EP

Gene names

Name:

DBI

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	87 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	Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.
Subunit structure	Monomer.
Subcellular location	Endoplasmic reticulum. Golgi apparatus. Note: Golgi localization is dependent on ligand binding. Ref.4 Ref.14
Tissue specificity	Isoform 1 is ubiquitous, with a moderate expression level. Isoform 2 is ubiquitous with high level in liver and adipose tissue. Isoform 3 is ubiquitous with strong expression in adipose tissue and heart. Ref.3 Ref.4
Sequence similarities	Belongs to the ACBP family. Contains 1 ACB (acyl-CoA-binding) domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Endoplasmic reticulum Golgi apparatus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	hair follicle development Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara transport Inferred from electronic annotation. Source: UniProtKB-KW triglyceride metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	benzodiazepine receptor binding Traceable author statement Ref.1. Source: ProtInc fatty-acyl-CoA binding Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: P07108-1)

Also known as: ACBP-1a; Short;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P07108-2)

Also known as: ACBP-1b; Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MWGDLWLLPPASANPGTGTE

Isoform 3 (identifier: P07108-3)

Also known as: ACBP-1c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MPAF

Isoform 4 (identifier: P07108-4)

Also known as: ACBP-1a1-g;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE

Isoform 5 (identifier: P07108-5)

Also known as: ACBP-1g;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE

Isoform 6 (identifier: P07108-6)

Also known as: ACBP-1e;

The sequence of this isoform differs from the canonical sequence as follows:
     43-87: ERPGMLDFTG...VEELKKKYGI → GMQSGGWKGI...YWPSPAATLY

Note: Predominantly expressed in adipose tissue and hippocampus.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10 Ref.11

Chain

2 – 87

86

Acyl-CoA-binding protein

PRO_0000214004

Regions

Domain

2 – 87

86

ACB

Region

29 – 33

5

Acyl-CoA binding

Sites

Binding site

14

1

Acyl-CoA

Binding site

55

1

Acyl-CoA

Binding site

74

1

Acyl-CoA

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.10 Ref.15

Modified residue

8

1

N6-acetyllysine Ref.15

Modified residue

19

1

N6-acetyllysine Ref.15

Modified residue

29

1

Phosphotyrosine Ref.16

Modified residue

55

1

N6-acetyllysine; alternate Ref.15

Modified residue

55

1

N6-malonyllysine; alternate Ref.18

Modified residue

77

1

N6-acetyllysine Ref.15

Natural variations

Alternative sequence

1 – 3

3

MSQ → MWGDLWLLPPASANPGTGTE in isoform 2.

VSP_000068

Alternative sequence

1 – 3

3

MSQ → MPAF in isoform 3.

VSP_038680

Alternative sequence

1 – 3

3

MSQ → MSQHRAGRRGGVGKRGVRGR ELGGQGKYGAGCSECGTRRI AARGE in isoform 4.

VSP_043437

Alternative sequence

1 – 3

3

MSQ → MERWGKGLHGLEERGDSVPI PKHRAGRRGGVGKRGVRGRE LGGQGKYGAGCSECGTRRIA ARGE in isoform 5.

VSP_043438

Alternative sequence

43 – 87

45

ERPGM…KKYGI → GMQSGGWKGICSSKQAQQLR LEVPGNFTLKLPEALLFRWG MVMVPEVEKTMFRILSVSSS NRIQILVLEGLYWPSPAATL Y in isoform 6.

VSP_044114

Natural variant

39

1

D → N.
Corresponds to variant rs8192504 [ dbSNP | Ensembl ].

VAR_048160

Natural variant

71

1

M → V.
Corresponds to variant rs8192506 [ dbSNP | Ensembl ].

VAR_048161

Natural variant

86

1

G → R.
Corresponds to variant rs8192507 [ dbSNP | Ensembl ].

VAR_048162

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

87

Helix Strand Turn

Details...

Helix

3 – 12

10

Helix

13 – 15

3

Helix

22 – 36

15

Helix

50 – 60

11

Turn

61 – 64

4

Helix

67 – 85

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ACBP-1a) (Short) [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B343A309F1B1AE28	FASTA	87	10,044
	10 20 30 40 50 60 MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN 70 80 ELKGTSKEDA MKAYINKVEE LKKKYGI
	Isoform 2 (ACBP-1b) (Long) [UniParc]. Checksum: 54D0238ABE40BCD2	FASTA	104	11,793
	10 20 30 40 50 60 MWGDLWLLPP ASANPGTGTE AEFEKAAEEV RHLKTKPSDE EMLFIYGHYK QATVGDINTE 70 80 90 100 RPGMLDFTGK AKWDAWNELK GTSKEDAMKA YINKVEELKK KYGI
	Isoform 3 (ACBP-1c) [UniParc]. Checksum: F4FFCEBA6D9D4330	FASTA	88	10,145
	10 20 30 40 50 60 MPAFAEFEKA AEEVRHLKTK PSDEEMLFIY GHYKQATVGD INTERPGMLD FTGKAKWDAW 70 80 NELKGTSKED AMKAYINKVE ELKKKYGI
	Isoform 4 (ACBP-1a1-g) [UniParc]. Checksum: A3985333C4BE1F8F	FASTA	129	14,367
	10 20 30 40 50 60 MSQHRAGRRG GVGKRGVRGR ELGGQGKYGA GCSECGTRRI AARGEAEFEK AAEEVRHLKT 70 80 90 100 110 120 KPSDEEMLFI YGHYKQATVG DINTERPGML DFTGKAKWDA WNELKGTSKE DAMKAYINKV EELKKKYGI
	Isoform 5 (ACBP-1g) [UniParc]. Checksum: 29F51D3DA08F300B	FASTA	148	16,495
	10 20 30 40 50 60 MERWGKGLHG LEERGDSVPI PKHRAGRRGG VGKRGVRGRE LGGQGKYGAG CSECGTRRIA 70 80 90 100 110 120 ARGEAEFEKA AEEVRHLKTK PSDEEMLFIY GHYKQATVGD INTERPGMLD FTGKAKWDAW 130 140 NELKGTSKED AMKAYINKVE ELKKKYGI
	Isoform 6 (ACBP-1e) [UniParc]. Checksum: 61407128B4E7B1DD	FASTA	123	13,911
	10 20 30 40 50 60 MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTGMQSGGWK GICSSKQAQQ 70 80 90 100 110 120 LRLEVPGNFT LKLPEALLFR WGMVMVPEVE KTMFRILSVS SSNRIQILVL EGLYWPSPAA TLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor." Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E. Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand." Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J., Lee D.C. DNA 6:71-79(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Identification of new acyl-CoA binding protein transcripts in human and mouse." Nitz I., Doering F., Schrezenmeir J., Burwinkel B. Int. J. Biochem. Cell Biol. 37:2395-2405(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
[4]	"Identification of a novel human Acyl-CoA binding protein isoform with a unique C-terminal domain." Ludewig A.H., Nitz I., Klapper M., Doring F. IUBMB Life 63:547-552(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"Specific regulation of low-abundance transcript variants encoding human Acyl-CoA binding protein (ACBP) isoforms." Nitz I., Kruse M.L., Klapper M., Doring F. J. Cell. Mol. Med. 15:909-927(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE.
[6]	"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] (ISOFORM 1).
[7]	"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].
[8]	Mural R.J., Istrail S., Sutton 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].
[9]	"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] (ISOFORMS 1 AND 2). Tissue: Brain.
[10]	"Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor." Marquardt H., Todaro G.J., Shoyab M. J. Biol. Chem. 261:9727-9731(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), ACETYLATION AT SER-2. Tissue: Brain.
[11]	"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 2-14 (ISOFORM 1). Tissue: Platelet.
[12]	"Purification and analysis of growth regulating proteins secreted by a human melanoma cell line." Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U. Melanoma Res. 2:327-336(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-30 AND 72-87.
[13]	"The characterization of two diazepam binding inhibitor (DBI) transcripts in humans." Kolmer M., Rovio A., Alho H. Biochem. J. 306:327-330(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[14]	"Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells." Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J. Biochem. J. 410:463-472(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8; LYS-19; LYS-55 AND LYS-77, MASS SPECTROMETRY.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-55.
[19]	"High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand." Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K. Proteins 66:229-238(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14200 mRNA. Translation: AAA52171.1.
M15887 mRNA. Translation: AAA35788.1.
FM213123 mRNA. Translation: CAR82405.1.
FM213124 mRNA. Translation: CAR82406.1.
FM213125 mRNA. Translation: CAR82407.1.
FM213126 mRNA. Translation: CAR82408.1.
FM213127 mRNA. Translation: CAR82409.1.
FM213128 mRNA. Translation: CAR82410.1.
FM213131 mRNA. Translation: CAR82414.1.
CR456956 mRNA. Translation: CAG33237.1.
AC016736 Genomic DNA. Translation: AAY14873.1.
CH471103 Genomic DNA. Translation: EAW95214.1.
BC006466 mRNA. No translation available.
BC062996 mRNA. Translation: AAH62996.1.
AM000001 mRNA. Translation: CAJ00736.1.

IPI

IPI00010182.
IPI00218836.
IPI00921830.
IPI00922055.
IPI00965476.

PIR

NZHU. B26448.

RefSeq

NP_001073331.1. NM_001079862.1.
NP_001073332.1. NM_001079863.1.
NP_001171488.1. NM_001178017.1.
NP_001171512.1. NM_001178041.1.
NP_001171513.1. NM_001178042.1.
NP_001171514.1. NM_001178043.1.
NP_065438.1. NM_020548.6.

UniGene

Hs.78888.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CB8	X-ray	1.40	A/B	1-87	[»]
2FJ9	X-ray	1.60	A	2-87	[»]

ProteinModelPortal

P07108.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07108. 1 interaction.

MINT

MINT-1394907.

STRING

9606.ENSP00000311117.

PTM databases

PhosphoSite

P07108.

Polymorphism databases

DMDM

118276.

Proteomic databases

PaxDb

P07108.

PRIDE

P07108.

Protocols and materials databases

DNASU

1622.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311521; ENSP00000311117; ENSG00000155368.
ENST00000355857; ENSP00000348116; ENSG00000155368.
ENST00000393103; ENSP00000376815; ENSG00000155368.
ENST00000409094; ENSP00000386486; ENSG00000155368.
ENST00000535617; ENSP00000442917; ENSG00000155368.
ENST00000535757; ENSP00000439012; ENSG00000155368.
ENST00000542275; ENSP00000440698; ENSG00000155368.

GeneID

1622.

KEGG

hsa:1622.

UCSC

uc002tlv.3. human.
uc002tlx.3. human.

Organism-specific databases

CTD

1622.

GeneCards

GC02P120124.

HGNC

HGNC:2690. DBI.

HPA

CAB008595.

MIM

125950. gene.

neXtProt

NX_P07108.

PharmGKB

PA27158.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4281.

HOVERGEN

HBG000398.

KO

K08762.

OMA

GDNTTDK.

OrthoDB

EOG4GF3GS.

Gene expression databases

ArrayExpress

P07108.

Bgee

P07108.

CleanEx

HS_DBI.

Genevestigator

P07108.

GermOnline

ENSG00000155368. Homo sapiens.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.

InterPro

IPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]

Pfam

PF00887. ACBP. 1 hit.
[Graphical view]

PRINTS

PR00689. ACOABINDINGP.

SUPFAM

SSF47027. ACBP. 1 hit.

PROSITE

PS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DBI. human.

EvolutionaryTrace

P07108.

GenomeRNAi

1622.

NextBio

6658.

SOURCE

Search...

Entry information

Entry name

ACBP_HUMAN

Accession

Primary (citable) accession number: P07108
Secondary accession number(s): B8ZWD2 , B8ZWD6, B8ZWD7, P08869, Q4VWZ6, Q53SQ7, Q6IB48, Q9UCI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 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.