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   24-JAN-2024, entry version 177.
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; 7.
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   MaxQB; 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; 197 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.
DR   Genevisible; P55001; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   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
//