ID   MFAP2_MOUSE             Reviewed;         183 AA.
AC   P55002;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 133.
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=Magp, Magp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RX   PubMed=8262979; DOI=10.1016/s0021-9258(19)74260-4;
RA   Chen Y., Faraco J., Yin W., Germiller J., Francke U., Bonadio J.;
RT   "Structure, chromosomal localization, and expression pattern of the murine
RT   Magp gene.";
RL   J. Biol. Chem. 268:27381-27389(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MFAP family. {ECO:0000305}.
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DR   EMBL; L23769; AAA16448.1; -; mRNA.
DR   EMBL; BC035490; AAH35490.1; -; mRNA.
DR   CCDS; CCDS18860.2; -.
DR   PIR; A49313; A49313.
DR   RefSeq; NP_001155271.1; NM_001161799.1.
DR   RefSeq; NP_032572.2; NM_008546.3.
DR   AlphaFoldDB; P55002; -.
DR   STRING; 10090.ENSMUSP00000071868; -.
DR   iPTMnet; P55002; -.
DR   PhosphoSitePlus; P55002; -.
DR   MaxQB; P55002; -.
DR   PaxDb; P55002; -.
DR   PeptideAtlas; P55002; -.
DR   PRIDE; P55002; -.
DR   ProteomicsDB; 292226; -.
DR   DNASU; 17150; -.
DR   GeneID; 17150; -.
DR   KEGG; mmu:17150; -.
DR   CTD; 4237; -.
DR   MGI; MGI:99559; Mfap2.
DR   eggNOG; ENOG502RXC2; Eukaryota.
DR   InParanoid; P55002; -.
DR   Reactome; R-MMU-1566948; Elastic fibre formation.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   ChiTaRS; Mfap2; mouse.
DR   PRO; PR:P55002; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P55002; protein.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0001527; C:microfibril; IDA:MGI.
DR   GO; GO:0070051; F:fibrinogen binding; IDA:MGI.
DR   GO; GO:0001968; F:fibronectin binding; IPI:MGI.
DR   GO; GO:0048048; P:embryonic eye morphogenesis; IBA:GO_Central.
DR   GO; GO:0030220; P:platelet formation; IMP:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   InterPro; IPR008673; MAGP.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR16485; PTHR16485; 1.
DR   Pfam; PF05507; MAGP; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Sulfation.
FT   SIGNAL          1..16
FT                   /note="Or 18"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..183
FT                   /note="Microfibrillar-associated protein 2"
FT                   /id="PRO_0000018683"
FT   DOMAIN          153..183
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   REGION          52..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P27424"
FT   MOD_RES         46
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P27424"
FT   MOD_RES         47
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P27424"
FT   MOD_RES         49
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"
SQ   SEQUENCE   183 AA;  20578 MW;  1F193F2BE2EF1D05 CRC64;
     MRAACLFLLF MPGLLAQGQY DLDPLPPFPD HVQYNHYGDQ IDNADYYDYQ EVSPRTPEEQ
     FQSQQQVQQE VIPAPTPEPA AAGDLETEPT EPGPLDCREE QYPCTRLYSI HKPCKQCLNE
     VCFYSLRRVY VVNKEICVRT VCAHEELLRA DLCRDKFSKC GVMAVSGLCQ SVAASCARSC
     GGC