ID MFAP4_HUMAN Reviewed; 255 AA. AC P55083; Q6P680; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 16-JUN-2009, entry version 69. DE RecName: Full=Microfibril-associated glycoprotein 4; DE Flags: Precursor; GN Name=MFAP4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=95359962; PubMed=7633408; DOI=10.1093/hmg/4.4.589; RA Zhao Z., Lee C.-C., Jiralerspong S., Juyal R.C., Lu F., Baldini A., RA Greenberg F., Caskey C.T., Patel P.I.; RT "The gene for a human microfibril-associated glycoprotein is commonly RT deleted in Smith-Magenis syndrome patients."; RL Hum. Mol. Genet. 4:589-597(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=PNS; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 22-36. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-87 AND ASN-137, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). CC -!- FUNCTION: Could be involved in calcium-dependent cell adhesion or CC intercellular interactions. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- DISEASE: MFAP4 is deleted in the Smith-Magenis syndrome (SMS) CC [MIM:182290]. CC -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38486; AAB00968.1; ALT_INIT; mRNA. DR EMBL; BC062415; AAH62415.1; -; mRNA. DR IPI; IPI00022792; -. DR RefSeq; NP_002395.1; -. DR UniGene; Hs.296049; -. DR HSSP; P02671; 1FZD. DR PRIDE; P55083; -. DR Ensembl; ENSG00000166482; Homo sapiens. DR GeneID; 4239; -. DR KEGG; hsa:4239; -. DR GeneCards; GC17M019227; -. DR H-InvDB; HIX0039181; -. DR HGNC; HGNC:7035; MFAP4. DR MIM; 182290; phenotype. DR MIM; 600596; gene. DR Orphanet; 819; Smith-Magenis syndrome. DR PharmGKB; PA30771; -. DR HOGENOM; P55083; -. DR HOVERGEN; P55083; -. DR NextBio; 16715; -. DR Bgee; P55083; -. DR CleanEx; HS_MFAP4; -. DR GermOnline; ENSG00000166482; Homo sapiens. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0001527; C:microfibril; NAS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005102; F:receptor binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR002181; Fibrinogen_a/b/g_C. DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1. DR Gene3D; G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1. DR Pfam; PF00147; Fibrinogen_C; 1. DR SMART; SM00186; FBG; 1. DR PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. PE 1: Evidence at protein level; KW Calcium; Cell adhesion; Direct protein sequencing; KW Extracellular matrix; Glycoprotein; Secreted; Signal. FT SIGNAL 1 21 FT CHAIN 22 255 Microfibril-associated glycoprotein 4. FT /FTId=PRO_0000009134. FT DOMAIN 32 255 Fibrinogen C-terminal. FT MOTIF 26 28 Cell attachment site (Potential). FT CARBOHYD 87 87 N-linked (GlcNAc...). FT CARBOHYD 137 137 N-linked (GlcNAc...). FT CONFLICT 173 173 A -> V (in Ref. 2; AAH62415). SQ SEQUENCE 255 AA; 28648 MW; B8F0B47AC694435E CRC64; MKALLALPLL LLLSTPPCAP QVSGIRGDAL ERFCLQQPLD CDDIYAQGYQ SDGVYLIYPS GPSVPVPVFC DMTTEGGKWT VFQKRFNGSV SFFRGWNDYK LGFGRADGEY WLGLQNMHLL TLKQKYELRV DLEDFENNTA YAKYADFSIS PNAVSAEEDG YTLFVAGFED GGAGDSLSYH SGQKFSTFDR DQDLFVQNCA ALSSGAFWFR SCHFANLNGF YLGGSHLSYA NGINWAQWKG FYYSLKRTEM KIRRA //