ID MFAP2_HUMAN Reviewed; 183 AA. AC P55001; Q53X60; Q5JXY0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-OCT-2024, entry version 180. DE RecName: Full=Microfibrillar-associated protein 2; DE Short=MFAP-2; DE AltName: Full=Microfibril-associated glycoprotein 1; DE Short=MAGP; DE Short=MAGP-1; DE Flags: Precursor; GN Name=MFAP2; Synonyms=MAGP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=7759096; DOI=10.1016/0888-7543(95)80004-6; RA Faraco J., Bashir M.M., Rosenbloom J., Francke U.; RT "Characterization of the human gene for microfibril-associated glycoprotein RT (MFAP2), assignment to chromosome 1p36.1-p35, and linkage to D1S170."; RL Genomics 25:630-637(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A'). RC TISSUE=Dermoid cancer; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Uterus; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-99 (ISOFORM B). RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M., RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L., RA Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A., RA Wohldmann P., Wilson R.; RT "The WashU-Merck EST project."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP ALTERNATIVE SPLICING. RX PubMed=11102756; DOI=10.1016/s0945-053x(00)00115-3; RA Segade F., Broekelmann T.J., Pierce R.A., Mecham R.P.; RT "Revised genomic structure of the human MAGP1 gene and identification of RT alternate transcripts in human and mouse tissues."; RL Matrix Biol. 19:671-682(2000). CC -!- FUNCTION: Component of the elastin-associated microfibrils. CC -!- SUBUNIT: Forms a ternary complex with BGN and ELN. Interacts with FBN1 CC (via N-terminal domain) and FBN2. {ECO:0000250|UniProtKB:P27424}. CC -!- INTERACTION: CC P55001; P49639: HOXA1; NbExp=3; IntAct=EBI-2462387, EBI-740785; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=P55001-1; Sequence=Displayed; CC Name=A'; CC IsoId=P55001-2; Sequence=VSP_042780; CC Name=B; CC IsoId=P55001-3; Sequence=VSP_042779; CC -!- PTM: Forms intermolecular disulfide bonds either with other MAGP-1 CC molecules or with other components of the microfibrils. May form CC transglutaminase cross-links. CC -!- PTM: O-glycosylated. CC -!- SIMILARITY: Belongs to the MFAP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U19718; AAA79920.1; -; mRNA. DR EMBL; CR407678; CAG28606.1; -; mRNA. DR EMBL; AK222751; BAD96471.1; -; mRNA. DR EMBL; AL049569; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW94821.1; -; Genomic_DNA. DR EMBL; BC015039; AAH15039.1; -; mRNA. DR EMBL; H27217; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS174.1; -. [P55001-1] DR CCDS; CCDS44071.1; -. [P55001-2] DR PIR; I38923; I38923. DR RefSeq; NP_001128719.1; NM_001135247.1. [P55001-2] DR RefSeq; NP_001128720.1; NM_001135248.1. [P55001-2] DR RefSeq; NP_002394.1; NM_002403.3. [P55001-1] DR RefSeq; NP_059453.1; NM_017459.2. [P55001-1] DR RefSeq; XP_011539778.1; XM_011541476.2. DR AlphaFoldDB; P55001; -. DR BioGRID; 110395; 8. DR IntAct; P55001; 1. DR STRING; 9606.ENSP00000364685; -. DR GlyCosmos; P55001; 2 sites, 2 glycans. DR GlyGen; P55001; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P55001; -. DR PhosphoSitePlus; P55001; -. DR BioMuta; MFAP2; -. DR DMDM; 1708914; -. DR jPOST; P55001; -. DR MassIVE; P55001; -. DR PaxDb; 9606-ENSP00000364685; -. DR PeptideAtlas; P55001; -. DR ProteomicsDB; 56750; -. [P55001-1] DR ProteomicsDB; 56751; -. [P55001-2] DR ProteomicsDB; 56752; -. [P55001-3] DR Pumba; P55001; -. DR Antibodypedia; 1230; 191 antibodies from 23 providers. DR DNASU; 4237; -. DR Ensembl; ENST00000375534.7; ENSP00000364684.3; ENSG00000117122.14. [P55001-2] DR Ensembl; ENST00000375535.4; ENSP00000364685.3; ENSG00000117122.14. [P55001-1] DR GeneID; 4237; -. DR KEGG; hsa:4237; -. DR MANE-Select; ENST00000375535.4; ENSP00000364685.3; NM_002403.4; NP_002394.1. DR UCSC; uc001azw.4; human. [P55001-1] DR AGR; HGNC:7033; -. DR CTD; 4237; -. DR DisGeNET; 4237; -. DR GeneCards; MFAP2; -. DR HGNC; HGNC:7033; MFAP2. DR HPA; ENSG00000117122; Low tissue specificity. DR MIM; 156790; gene. DR neXtProt; NX_P55001; -. DR OpenTargets; ENSG00000117122; -. DR PharmGKB; PA30769; -. DR VEuPathDB; HostDB:ENSG00000117122; -. DR eggNOG; ENOG502RXC2; Eukaryota. DR GeneTree; ENSGT00390000017736; -. DR HOGENOM; CLU_124750_0_0_1; -. DR InParanoid; P55001; -. DR OMA; CMRTVCA; -. DR OrthoDB; 4636829at2759; -. DR PhylomeDB; P55001; -. DR TreeFam; TF333418; -. DR PathwayCommons; P55001; -. DR Reactome; R-HSA-1566948; Elastic fibre formation. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR SignaLink; P55001; -. DR BioGRID-ORCS; 4237; 9 hits in 1140 CRISPR screens. DR GeneWiki; MFAP2; -. DR GenomeRNAi; 4237; -. DR Pharos; P55001; Tbio. DR PRO; PR:P55001; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P55001; protein. DR Bgee; ENSG00000117122; Expressed in stromal cell of endometrium and 97 other cell types or tissues. DR ExpressionAtlas; P55001; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0001527; C:microfibril; IDA:CACAO. DR GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl. DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl. DR GO; GO:0048048; P:embryonic eye morphogenesis; IEP:UniProtKB. DR GO; GO:0030220; P:platelet formation; IEA:Ensembl. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0048050; P:post-embryonic eye morphogenesis; IEP:UniProtKB. DR InterPro; IPR008673; MAGP. DR InterPro; IPR003582; ShKT_dom. DR PANTHER; PTHR16485; MICROFIBRILLAR-ASSOCIATED PROTEIN 2; 1. DR PANTHER; PTHR16485:SF3; MICROFIBRILLAR-ASSOCIATED PROTEIN 2; 1. DR Pfam; PF05507; MAGP; 1. DR PROSITE; PS51670; SHKT; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein; KW Proteomics identification; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal; Sulfation. FT SIGNAL 1..17 FT /note="Or 19" FT /evidence="ECO:0000255" FT CHAIN 18..183 FT /note="Microfibrillar-associated protein 2" FT /id="PRO_0000018682" FT DOMAIN 153..183 FT /note="ShKT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005" FT REGION 58..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..75 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 18 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P27424" FT MOD_RES 47 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250|UniProtKB:P27424" FT MOD_RES 48 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250|UniProtKB:P27424" FT MOD_RES 50 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250|UniProtKB:P27424" FT DISULFID 153..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005" FT DISULFID 160..176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005" FT DISULFID 169..180 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005" FT VAR_SEQ 13..42 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_042779" FT VAR_SEQ 13 FT /note="Missing (in isoform A')" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_042780" SQ SEQUENCE 183 AA; 20826 MW; A75BE15DC9629B26 CRC64; MRAAYLFLLF LPAGLLAQGQ YDLDPLPPFP DHVQYTHYSD QIDNPDYYDY QEVTPRPSEE QFQFQSQQQV QQEVIPAPTP EPGNAELEPT EPGPLDCREE QYPCTRLYSI HRPCKQCLNE VCFYSLRRVY VINKEICVRT VCAHEELLRA DLCRDKFSKC GVMASSGLCQ SVAASCARSC GSC //