Adipocyte, C1q and collagen domain-containing protein
30 kDa adipocyte complement-related protein
Adipocyte complement-related 30 kDa protein
ACRP30
Adipose most abundant gene transcript 1 protein
apM-1
Gelatin-binding protein

Gene name

	Name:	ADIPOQ
	Synonyms:	ACDC, ACRP30, APM1, GBP28

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adipose tissue; DOI=10.1006/bbrc.1996.0587; PubMed=8619847 [NCBI, ExPASy, EBI, Israel, Japan] Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., Matsubara K.; "cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)."; Biochem. Biophys. Res. Commun. 221:286-289(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0378-1119(99)00041-4; PubMed=10095105 [NCBI, ExPASy, EBI, Israel, Japan] Saito K., Tobe T., Minoshima S., Asakawa S., Sumiya J., Yoda M., Nakano Y., Shimizu N., Tomita M.; "Organization of the gene for gelatin-binding protein (GBP28)."; Gene 229:67-73(1999).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/bbrc.1999.0865; PubMed=10403784 [NCBI, ExPASy, EBI, Israel, Japan] Schaeffler A., Orso E., Palitzsch K.D., Buechler C., Drobnik W., Fuerst A., Schoelmerich J., Schmitz G.; "The human apM-1, an adipocyte-specific gene linked to the family of TNF's and to genes expressed in activated T cells, is mapped to chromosome 1q21.3-q23, a susceptibility locus identified for familial combined hyperlipidemia (FCH)."; Biochem. Biophys. Res. Commun. 260:416-425(1999).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 19-33. DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Henzel W.J.; "Signal peptide prediction based on analysis of experimentally verified cleavage sites."; Protein Sci. 13:2819-2824(2004).
[6]	PROTEIN SEQUENCE OF N-TERMINUS, AND PARTIAL PROTEIN SEQUENCE. PubMed=8947845 [NCBI, ExPASy, EBI, Israel, Japan] Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M.; "Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma."; J. Biochem. 120:803-812(1996).
[7]	CHARACTERIZATION. PubMed=10961870 [NCBI, ExPASy, EBI, Israel, Japan] Yokota T., Oritani K., Takahashi I., Ishikawa J., Matsuyama A., Ouchi N., Kihara S., Funahashi T., Tenner A.J., Tomiyama Y., Matsuzawa Y.; "Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages."; Blood 96:1723-1732(2000).
[8]	CHARACTERIZATION. PubMed=10982546 [NCBI, ExPASy, EBI, Israel, Japan] Ouchi N., Kihara S., Arita Y., Okamoto Y., Maeda K., Kuriyama H., Hotta K., Nishida M., Takahashi M., Muraguchi M., Ohmoto Y., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y.; "Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-kappaB signaling through a cAMP-dependent pathway."; Circulation 102:1296-1301(2000).
[9]	FUNCTION. DOI=10.1038/90984; PubMed=11479627 [NCBI, ExPASy, EBI, Israel, Japan] Yamauchi T., Kamon J., Waki H., Terauchi Y., Kubota N., Hara K., Mori Y., Ide T., Murakami K., Tsuboyama-Kasaoka N., Ezaki O., Akanuma Y., Gavrilova O., Vinson C., Reitman M.L., Kagechika H., Shudo K., Yoda M., Nakano Y., Tobe K., Nagai R., Kimura S., Tomita M., Froguel P., Kadowaki T.; "The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity."; Nat. Med. 7:941-946(2001).
[10]	SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-36, AND CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164. DOI=10.1074/jbc.M300365200; PubMed=12878598 [NCBI, ExPASy, EBI, Israel, Japan] Waki H., Yamauchi T., Kamon J., Ito Y., Uchida S., Kita S., Hara K., Hada Y., Vasseur F., Froguel P., Kimura S., Nagai R., Kadowaki T.; "Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin."; J. Biol. Chem. 278:40352-40363(2003).
[11]	SUBUNIT, HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68; PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101, GLYCOSYLATION AT LYS-65; LYS-68; LYS-77 AND LYS-101, DISULFIDE BOND, ABSENCE OF HYDROXYLATION AT PRO-62; PRO-86 AND PRO-104, ABSENCE OF GLYCOSYLATION AT ASN-230, MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 AND LYS-101, AND MASS SPECTROMETRY. DOI=10.1210/me.2005-0390; PubMed=16497731 [NCBI, ExPASy, EBI, Israel, Japan] Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., Whitehead J.P.; "Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications."; Mol. Endocrinol. 20:1673-1687(2006).
[12]	VARIANT ADPND CYS-112. DOI=10.1038/sj.ijo.0801244; PubMed=10918532 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi M., Arita Y., Yamagata K., Matsukawa Y., Okutomi K., Horie M., Shimomura I., Hotta K., Kuriyama H., Kihara S., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y.; "Genomic structure and mutations in adipose-specific gene, adiponectin."; Int. J. Obes. Relat. Metab. Disord. 24:861-868(2000).
[13]	VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241. PubMed=11812766 [NCBI, ExPASy, EBI, Israel, Japan] Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M., Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T.; "Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population."; Diabetes 51:536-540(2002).
[14]	ERRATUM. Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M., Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T.; Diabetes 51:1294-1294(2002).
[15]	VARIANTS CYS-112; THR-164; SER-221 AND PRO-241, AND ASSOCIATION WITH LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2. PubMed=12086969 [NCBI, ExPASy, EBI, Israel, Japan] Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M., Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S., Funahashi T., Matsuzawa Y.; "Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome."; Diabetes 51:2325-2328(2002).
[16]	VARIANTS ARG-84; SER-90 AND HIS-111. DOI=10.1093/hmg/11.21.2607; PubMed=12354786 [NCBI, ExPASy, EBI, Israel, Japan] Vasseur F., Helbecque N., Dina C., Lobbens S., Delannoy V., Gaget S., Boutin P., Vaxillaire M., Lepretre F., Dupont S., Hara K., Clement K., Bihain B., Kadowaki T., Froguel P.; "Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians."; Hum. Mol. Genet. 11:2607-2614(2002).

Comments

FUNCTION: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.
SUBUNIT: Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionnally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and secreted into plasma.
DOMAIN: The C1q domain is commonly called the globular domain.
PTM: Hydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting.
PTM: HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes (By similarity).
PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
PTM: Not N-glycosylated.
POLYMORPHISM: Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIM:612556].
DISEASE: Defects in ADIPOQ are the cause of adiponectin deficiency (ADPND) [MIM:612556]. ADPND results in very low concentrations of plasma adiponectin.
DISEASE: Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance.
PHARMACEUTICAL: Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.
MISCELLANEOUS: Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form.
MISCELLANEOUS: HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion (By similarity). In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.
SIMILARITY: Contains 1 C1q domain.
SIMILARITY: Contains 1 collagen-like domain.
WEB RESOURCE: Name=Wikipedia; Note=Adiponectin entry; URL="http://en.wikipedia.org/wiki/Adiponectin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D45371; BAA08227.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB012165; BAA86716.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ131460; CAB52413.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ131461; CAB52413.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054496; AAH54496.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096308; AAH96308.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096309; AAH96309.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096310; AAH96310.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096311; AAH96311.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00020019; -.

JC4708; JC4708.

NP_004788.1; -.

3D structure databases

HSSP

Q60994; 1C28. [HSSP ENTRY / PDB]

SMR

Q15848; 108-244.

ModBase

Q15848.

Organism-specific databases

GC03P188044; -.

HIX0020222; -.

HGNC:13633; ADIPOQ.

125853; phenotype. [NCBI / EBI]
605441; gene. [NCBI / EBI]
612556; phenotype. [NCBI / EBI]

PharmGKB

PA134933118; -.

Gene expression databases

Q15848; -.

Q15848; -.

HS_ADIPOQ; -.

ENSG00000181092; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005125;	Molecular function: cytokine activity (non-traceable author statement from UniProtKB).
GO:0043499;	Molecular function: eukaryotic cell surface binding (inferred from direct assay from UniProtKB).
GO:0005179;	Molecular function: hormone activity (inferred from direct assay from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from sequence or structural similarity from UniProtKB).
GO:0006091;	Biological process: generation of precursor metabolites and energy (traceable author statement from ProtInc).
GO:0042593;	Biological process: glucose homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0006006;	Biological process: glucose metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0034383;	Biological process: low-density lipoprotein particle clearance (inferred from direct assay from UniProtKB).
GO:0045599;	Biological process: negative regulation of fat cell differentiation (inferred from direct assay from UniProtKB).
GO:0010745;	Biological process: negative regulation of foam cell differentiation (inferred from direct assay from UniProtKB).
GO:0045721;	Biological process: negative regulation of gluconeogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0030853;	Biological process: negative regulation of granulocyte differentiation (inferred from direct assay from UniProtKB).
GO:0034115;	Biological process: negative regulation of heterotypic cell-cell adhesion (inferred from direct assay from UniProtKB).
GO:0043124;	Biological process: negative regulation of I-kappaB kinase/NF-kappaB cascade (inferred from direct assay from UniProtKB).
GO:0050728;	Biological process: negative regulation of inflammatory response (non-traceable author statement from UniProtKB).
GO:0045715;	Biological process: negative regulation of low-density lipoprotein receptor biosynthetic process (inferred from direct assay from UniProtKB).
GO:0050765;	Biological process: negative regulation of phagocytosis (inferred from direct assay from UniProtKB).
GO:0010804;	Biological process: negative regulation of tumor necrosis factor-mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0032720;	Biological process: negative regulation of tumor necrosis factor production (inferred from direct assay from UniProtKB).
GO:0032270;	Biological process: positive regulation of cellular protein metabolic process (inferred from direct assay from UniProtKB).
GO:0010875;	Biological process: positive regulation of cholesterol efflux (inferred from direct assay from UniProtKB).
GO:0045923;	Biological process: positive regulation of fatty acid metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0046326;	Biological process: positive regulation of glucose import (inferred from sequence or structural similarity from UniProtKB).
GO:0033034;	Biological process: positive regulation of myeloid cell apoptosis (inferred from direct assay from UniProtKB).
GO:0010739;	Biological process: positive regulation of protein kinase A signaling cascade (inferred from direct assay from UniProtKB).
GO:0009749;	Biological process: response to glucose stimulus (inferred from sequence or structural similarity from UniProtKB).
GO:0034612;	Biological process: response to tumor necrosis factor (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001073; C1q.
IPR008160; Collagen.
IPR008983; Tumour_necrosis_fac-like.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.40; Tumour_necrosis_fac-like; 1.

Pfam

PF00386; C1q; 1.
PF01391; Collagen; 1.
Pfam graphical view of domain structure.

PRINTS

PR00007; COMPLEMNTC1Q.

ProDom

PD000007; Clg_helix; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00110; C1Q; 1.
SMART graphical view of domain structure.

PROSITE

PS50871; C1Q; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q15848; -.

PRIDE

Q15848; -.

Genome annotation databases

Ensembl

ENSG00000181092; Homo sapiens. [Contig view]

GeneID

9370; -.

KEGG

hsa:9370; -.

Phylogenomic databases

HOGENOM

Q15848; -.

HOVERGEN

Q15848; -.

OMA

Q15848; YHITVYM.

Other

NextBio

35094; -.

SOURCE

ADIPOQ; Homo sapiens.

ProtoNet

Q15848.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Collagen; Diabetes mellitus; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hormone; Hydroxylation; Obesity; Pharmaceutical; Polymorphism; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 244`	`226`	`Adiponectin.`	`PRO_0000003543`
`DOMAIN`	`42 107`	`66`	`Collagen-like.`
`DOMAIN`	`108 244`	`137`	`C1q.`
`SITE`	`62 62`	`1`	`Not hydroxylated.`
`SITE`	`86 86`	`1`	`Not hydroxylated.`
`SITE`	`104 104`	`1`	`Not hydroxylated.`
`SITE`	`230 230`	`1`	`Not glycosylated.`
`MOD_RES`	`33 33`		`5-hydroxylysine (Probable).`
`MOD_RES`	`44 44`		`4-hydroxyproline.`
`MOD_RES`	`47 47`		`4-hydroxyproline.`
`MOD_RES`	`53 53`		`4-hydroxyproline.`
`MOD_RES`	`65 65`		`5-hydroxylysine.`
`MOD_RES`	`68 68`		`5-hydroxylysine.`
`MOD_RES`	`71 71`		`4-hydroxyproline; partial.`
`MOD_RES`	`76 76`		`4-hydroxyproline; partial.`
`MOD_RES`	`77 77`		`5-hydroxylysine.`
`MOD_RES`	`91 91`		`4-hydroxyproline.`
`MOD_RES`	`95 95`		`4-hydroxyproline; partial.`
`MOD_RES`	`101 101`		`5-hydroxylysine.`
`CARBOHYD`	`65 65`		`O-linked (Gal...); partial.`
`CARBOHYD`	`68 68`		`O-linked (Gal...); partial.`
`CARBOHYD`	`77 77`		`O-linked (Gal...); partial.`
`CARBOHYD`	`101 101`		`O-linked (Gal...); partial.`
`DISULFID`	`36 36`		`Interchain; in form MMW and form HMW.`
`VARIANT`	`84 84`	`1`	`G -> R (does not form high molecular weight multimers).`	`VAR_013273`
`VARIANT`	`90 90`	`1`	`G -> S (does not form high molecular weight multimers).`	`VAR_027395`
`VARIANT`	`111 111`	`1`	`Y -> H (in dbSNP:rs17366743 [NCBI]).`	`VAR_027396 [3D]`
`VARIANT`	`112 112`	`1`	`R -> C (in ADPND; does not assemble into trimers resulting in impaired secretion from the cell).`	`VAR_013274 [3D]`
`VARIANT`	`117 117`	`1`	`V -> M.`	`VAR_013275 [3D]`
`VARIANT`	`164 164`	`1`	`I -> T (associated with low plasma adiponectin concentration and diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell).`	`VAR_013276 [3D]`
`VARIANT`	`221 221`	`1`	`R -> S.`	`VAR_013277 [3D]`
`VARIANT`	`241 241`	`1`	`H -> P.`	`VAR_013278 [3D]`
`MUTAGEN`	`33 33`		`K->R: No effect on formation of HMW multimers.`
`MUTAGEN`	`36 36`		`C->S: Impaired formation of MMW and HMW multimers.`
`MUTAGEN`	`65 65`		`K->R: Impaired formation of HMW multimers; when associated with R-68.`
`MUTAGEN`	`68 68`		`K->R: Impaired formation of HMW multimers; when associated with R-65.`
`MUTAGEN`	`77 77`		`K->R: Impaired formation of HMW multimers; when associated with R-101.`
`MUTAGEN`	`101 101`		`K->R: Impaired formation of HMW multimers; when associated with R-77.`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 26414 Da [This is the MW of the unprocessed precursor]

CRC64: 64D8C6C1204B1018 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLLGAVLLL LALPGHDQET TTQGPGVLLP LPKGACTGWM AGIPGHPGHN GAPGRDGRDG 

        70         80         90        100        110        120 
TPGEKGEKGD PGLIGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE 

       130        140        150        160        170        180 
TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK 

       190        200        210        220        230        240 
AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY 


HDTN

Q15848 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools