MFAP2_BOVIN
ID MFAP2_BOVIN Reviewed; 183 AA.
AC P27424;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 109.
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 AltName: Full=Tropoelastin-binding protein;
DE Flags: Precursor;
GN Name=MFAP2; Synonyms=MAGP, MAGP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Nuchal ligament;
RX PubMed=2019589; DOI=10.1016/s0021-9258(20)89489-7;
RA Gibson M.A., Sandberg L.B., Grosso L.E., Cleary E.G.;
RT "Complementary DNA cloning establishes microfibril-associated glycoprotein
RT (MAGP) to be a discrete component of the elastin-associated microfibrils.";
RL J. Biol. Chem. 266:7596-7601(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AMINO-ACID COMPOSITION, AND PYROGLUTAMATE
RP FORMATION AT GLN-18.
RX PubMed=8286390; DOI=10.1021/bi00168a026;
RA Bashir M.M., Abrams W.R., Rosenbloom J., Kucich U., Bacarra M., Han M.D.,
RA Brown-Augsberger P., Mecham R.P., Rosenbloom J.;
RT "Microfibril-associated glycoprotein: characterization of the bovine gene
RT and of the recombinantly expressed protein.";
RL Biochemistry 33:593-600(1994).
RN [3]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=3015971; DOI=10.1016/s0021-9258(18)67403-4;
RA Gibson M.A., Hughes J.L., Fanning J.C., Cleary E.G.;
RT "The major antigen of elastin-associated microfibrils is a 31-kDa
RT glycoprotein.";
RL J. Biol. Chem. 261:11429-11436(1986).
RN [4]
RP INTERACTION WITH BGN AND ELN.
RX PubMed=11723132; DOI=10.1074/jbc.m109540200;
RA Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.;
RT "Molecular interactions of biglycan and decorin with elastic fiber
RT components: biglycan forms a ternary complex with tropoelastin and
RT microfibril-associated glycoprotein 1.";
RL J. Biol. Chem. 277:3950-3957(2002).
RN [5]
RP GLYCOSYLATION, SULFATION AT TYR-47; TYR-48 AND TYR-50, TRANSGLUTAMINATION
RP AT GLN-20, AND MUTAGENESIS OF GLN-20; GLN-34; GLN-41; TYR-47; TYR-48;
RP TYR-50; THR-54; THR-79 AND THR-90.
RX PubMed=11284693; DOI=10.1021/bi002738z;
RA Trask B.C., Broekelmann T., Ritty T.M., Trask T.M., Tisdale C.,
RA Mecham R.P.;
RT "Posttranslational modifications of microfibril associated glycoprotein-1
RT (MAGP-1).";
RL Biochemistry 40:4372-4380(2001).
RN [6]
RP INTERACTION WITH FBN1 AND FBN2.
RX PubMed=15131124; DOI=10.1074/jbc.m313672200;
RA Hanssen E., Hew F.H., Moore E., Gibson M.A.;
RT "MAGP-2 has multiple binding regions on fibrillins and has covalent
RT periodic association with fibrillin-containing microfibrils.";
RL J. Biol. Chem. 279:29185-29194(2004).
CC -!- FUNCTION: Component of the elastin-associated microfibrils.
CC -!- SUBUNIT: Forms a ternary complex with BGN and ELN (PubMed:11723132).
CC Interacts with FBN1 (via N-terminal domain) and FBN2 (PubMed:15131124).
CC {ECO:0000269|PubMed:11723132, ECO:0000269|PubMed:15131124}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: O-glycosylated; glycans consist of Gal(beta1-3)GalNAc.
CC {ECO:0000269|PubMed:11284693}.
CC -!- PTM: Forms intermolecular disulfide bonds either with other MAGP-1
CC molecules or with other components of the microfibrils.
CC -!- PTM: Forms transglutaminase cross-links with tropoelastin.
CC {ECO:0000269|PubMed:11284693}.
CC -!- SIMILARITY: Belongs to the MFAP family. {ECO:0000305}.
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DR EMBL; M59851; AAA62715.1; -; mRNA.
DR EMBL; S68064; AAB29686.1; -; mRNA.
DR PIR; A54151; A54151.
DR RefSeq; NP_776813.1; NM_174388.2.
DR AlphaFoldDB; P27424; -.
DR CORUM; P27424; -.
DR STRING; 9913.ENSBTAP00000004994; -.
DR GlyConnect; 368; 1 O-Linked glycan.
DR PaxDb; P27424; -.
DR PRIDE; P27424; -.
DR GeneID; 281912; -.
DR KEGG; bta:281912; -.
DR CTD; 4237; -.
DR eggNOG; ENOG502RXC2; Eukaryota.
DR InParanoid; P27424; -.
DR OrthoDB; 1270624at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001527; C:microfibril; IBA:GO_Central.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Isopeptide bond; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..17
FT CHAIN 18..183
FT /note="Microfibrillar-associated protein 2"
FT /id="PRO_0000018681"
FT DOMAIN 153..183
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8286390"
FT MOD_RES 47
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:11284693"
FT MOD_RES 48
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:11284693"
FT MOD_RES 50
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:11284693"
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 CROSSLNK 20
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 20
FT /note="Q->N: Completely abolishes transglutamination."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 34
FT /note="Q->N: Some decrease in transglutamination."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 41
FT /note="Q->N: Little effect on transglutamination."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 47
FT /note="Y->S: Loss of sulfation; when associated with S-48
FT and S-50."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 48
FT /note="Y->S: Loss of sulfation; when associated with S-47
FT and S-50."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 50
FT /note="Y->S: Loss of sulfation; when associated with S-47
FT and S-48."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 54
FT /note="T->V: No change in glycosylation levels."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 79
FT /note="T->V: No change in glycosylation levels."
FT /evidence="ECO:0000269|PubMed:11284693"
FT MUTAGEN 90
FT /note="T->V: No change in glycosylation levels."
FT /evidence="ECO:0000269|PubMed:11284693"
SQ SEQUENCE 183 AA; 20709 MW; 11AAB06F87C6DA1E CRC64;
MRAASLFLLF LPAGLLAQGQ YDLDPLPPYP DHVQYTHYSE QIENPDYYDY PEMTPRPPEE
QFQFQSQQQV QQEVIPAPTL EPGTVETEPT EPGPLDCREE QYPCTRLYSI HKPCKQCLNE
VCFYSLRRVY VVNKEICVRT VCAQEELLRA DLCRDKFSKC GVLASSGLCQ SVAAACARSC
GGC
