MFAP4_BOVIN
ID MFAP4_BOVIN Reviewed; 255 AA.
AC P55918; Q29S09; Q8HY48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Microfibril-associated glycoprotein 4;
DE AltName: Full=36 kDa microfibril-associated glycoprotein;
DE Short=36 kDa MAP;
DE Flags: Precursor;
GN Name=MFAP4;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-239.
RC TISSUE=Skin;
RA Asai-Coakwell M., Schmutz S.M., Berryere T.G.;
RT "An integrated BTA19 linkage map including MFAP4.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 33-62; 85-123 AND 126-184.
RC TISSUE=Aorta;
RX PubMed=8117283; DOI=10.1006/bbrc.1994.1178;
RA Kobayashi R., Mizutani A., Hidaka H.;
RT "Isolation and characterization of a 36-kDa microfibril-associated
RT glycoprotein by the newly synthesized isoquinolinesulfonamide affinity
RT chromatography.";
RL Biochem. Biophys. Res. Commun. 198:1262-1266(1994).
CC -!- FUNCTION: Could be involved in calcium-dependent cell adhesion or
CC intercellular interactions. May contribute to the elastic fiber
CC assembly and/or maintenance. {ECO:0000250|UniProtKB:P55083}.
CC -!- SUBUNIT: Homodimer. Can also form higher oligomers. Interacts with
CC FBN1, FBN2 and LOX. Interacts with COL1A1 in a Ca (2+)-dependent
CC manner. Interacts with ELN in a Ca (2+)-dependent manner; this
CC interaction promotes ELN self-assembly. {ECO:0000250|UniProtKB:P55083}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P55083}.
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DR EMBL; BC113263; AAI13264.1; -; mRNA.
DR EMBL; AY173052; AAN85410.1; -; mRNA.
DR RefSeq; NP_001073686.1; NM_001080217.1.
DR AlphaFoldDB; P55918; -.
DR SMR; P55918; -.
DR BioGRID; 159902; 1.
DR STRING; 9913.ENSBTAP00000008130; -.
DR PaxDb; P55918; -.
DR PeptideAtlas; P55918; -.
DR PRIDE; P55918; -.
DR Ensembl; ENSBTAT00000008130; ENSBTAP00000008130; ENSBTAG00000006187.
DR GeneID; 286766; -.
DR KEGG; bta:286766; -.
DR CTD; 4239; -.
DR VEuPathDB; HostDB:ENSBTAG00000006187; -.
DR VGNC; VGNC:31424; MFAP4.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000154615; -.
DR HOGENOM; CLU_038628_6_0_1; -.
DR InParanoid; P55918; -.
DR OMA; TAYAKYT; -.
DR OrthoDB; 952558at2759; -.
DR TreeFam; TF336658; -.
DR Reactome; R-BTA-2129379; Molecules associated with elastic fibres.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000006187; Expressed in trachea and 103 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0071953; C:elastic fiber; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001527; C:microfibril; IEA:Ensembl.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071493; P:cellular response to UV-B; IEA:Ensembl.
DR GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
DR GO; GO:0048251; P:elastic fiber assembly; IBA:GO_Central.
DR GO; GO:0010712; P:regulation of collagen metabolic process; IEA:Ensembl.
DR GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..255
FT /note="Microfibril-associated glycoprotein 4"
FT /id="PRO_0000009133"
FT DOMAIN 32..255
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT MOTIF 26..28
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28558 MW; 36E7F81DD3FFBD41 CRC64;
MEALLVLPLL LLLSAGPCAP QLLGIRGDAL EKSCLQLPLD CDDIYAQGYQ ADGVYLIYPS
GPSVPVPVFC DMTTEGGKWT VFQKRFNGSV SFFRGWNDYK LGFGRADGEY WLGLQNMHLL
TLKQKYELRV DLEDFENNTA FAKYADFSIS PNAVSAEEDG YTLYVSGFED GGAGDSLTYH
SGQKFSTFDR DQDLFVQNCA ALSSGAFWFR SCHFANLNGF YLGGSHLSYA NGINWAQWKG
FYYSLKRTEM KIRRA
