[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Placenta; DOI=10.1093/hmg/4.4.589; PubMed=7633408 [NCBI, ExPASy, EBI, Israel, Japan] Zhao Z., Lee C.-C., Jiralerspong S., Juyal R.C., Lu F., Baldini A., Greenberg F., Caskey C.T., Patel P.I.; "The gene for a human microfibril-associated glycoprotein is commonly deleted in Smith-Magenis syndrome patients."; Hum. Mol. Genet. 4:589-597(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=PNS; 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).
[3]	PROTEIN SEQUENCE OF 22-36. 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).
[4]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).

Comments

FUNCTION: Could be involved in calcium-dependent cell adhesion or intercellular interactions.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.
DISEASE: MFAP4 is deleted in the Smith-Magenis syndrome (SMS) [MIM:182290].
SIMILARITY: Contains 1 fibrinogen C-terminal domain.

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

L38486; AAB00968.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062415; AAH62415.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_002395.1; -.

UniGene

Hs.296049

3D structure databases

HSSP

P02671; 1FZD. [HSSP ENTRY / PDB]

ModBase

P55083.

Organism-specific databases

GC17M019227; -.

HIX0039181; -.

HGNC:7035; MFAP4.

182290; phenotype. [NCBI / EBI]
600596; gene. [NCBI / EBI]

Orphanet

819; Smith-Magenis syndrome.

PharmGKB

PA30771; -.

GeneCards

P55083.

Gene expression databases

CleanEx

HS_MFAP4; -.

GermOnline

ENSG00000166482; Homo sapiens.

Ontologies

GO:0001527;	Cellular component: microfibril (non-traceable author statement from UniProtKB).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005102;	Molecular function: receptor binding (inferred from electronic annotation from InterPro).
GO:0007155;	Biological process: cell adhesion (non-traceable author statement from UniProtKB).
GO:0007165;	Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.

Pfam

PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.

SMART

SM00186; FBG; 1.
SMART graphical view of domain structure.

PROSITE

PS00514; FIBRINOGEN_C_1; FALSE_NEG.
PS51406; FIBRINOGEN_C_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

P55083; -.

Genome annotation databases

Ensembl

ENSG00000166482; Homo sapiens. [Contig view]

GeneID

4239; -.

KEGG

hsa:4239; -.

Phylogenomic databases

HOGENOM

P55083; -.

HOVERGEN

P55083; -.

Other

16715; -.

MFAP4; Homo sapiens.

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

Keywords

Calcium; Cell adhesion; Direct protein sequencing; Extracellular matrix; Glycoprotein; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 255`	`234`	`Microfibril-associated glycoprotein 4.`	`PRO_0000009134`
`DOMAIN`	`32 255`	`224`	`Fibrinogen C-terminal.`
`MOTIF`	`26 28`	`3`	`Cell attachment site (Potential).`
`CARBOHYD`	`87 87`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`137 137`		`N-linked (GlcNAc...).`
`CONFLICT`	`173 173`		`A -> V (in Ref. 2; AAH62415).`

Sequence information

Length: 255 AA [This is the length of the unprocessed precursor]

Molecular weight: 28648 Da [This is the MW of the unprocessed precursor]

CRC64: B8F0B47AC694435E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKALLALPLL LLLSTPPCAP QVSGIRGDAL ERFCLQQPLD CDDIYAQGYQ SDGVYLIYPS 

        70         80         90        100        110        120 
GPSVPVPVFC DMTTEGGKWT VFQKRFNGSV SFFRGWNDYK LGFGRADGEY WLGLQNMHLL 

       130        140        150        160        170        180 
TLKQKYELRV DLEDFENNTA YAKYADFSIS PNAVSAEEDG YTLFVAGFED GGAGDSLSYH 

       190        200        210        220        230        240 
SGQKFSTFDR DQDLFVQNCA ALSSGAFWFR SCHFANLNGF YLGGSHLSYA NGINWAQWKG 

       250 
FYYSLKRTEM KIRRA

P55083 in FASTA format

View entry in original UniProtKB/Swiss-Prot 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