ID MFAP4_MOUSE Reviewed; 257 AA.
AC Q9D1H9; Q5NCN1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 158.
DE RecName: Full=Microfibril-associated glycoprotein 4;
DE Flags: Precursor;
GN Name=Mfap4;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D1H9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D1H9-2; Sequence=VSP_013482;
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; AK003537; BAB22844.1; -; mRNA.
DR EMBL; AL604029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022666; AAH22666.1; -; mRNA.
DR CCDS; CCDS24813.1; -. [Q9D1H9-1]
DR CCDS; CCDS83820.1; -. [Q9D1H9-2]
DR RefSeq; NP_001334474.1; NM_001347545.1. [Q9D1H9-2]
DR RefSeq; NP_083844.1; NM_029568.2. [Q9D1H9-1]
DR AlphaFoldDB; Q9D1H9; -.
DR SMR; Q9D1H9; -.
DR IntAct; Q9D1H9; 1.
DR STRING; 10090.ENSMUSP00000038971; -.
DR GlyConnect; 2512; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q9D1H9; 2 sites, 1 glycan.
DR GlyGen; Q9D1H9; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9D1H9; -.
DR PhosphoSitePlus; Q9D1H9; -.
DR CPTAC; non-CPTAC-3363; -.
DR MaxQB; Q9D1H9; -.
DR PaxDb; 10090-ENSMUSP00000070848; -.
DR PeptideAtlas; Q9D1H9; -.
DR ProteomicsDB; 295560; -. [Q9D1H9-1]
DR ProteomicsDB; 295561; -. [Q9D1H9-2]
DR Antibodypedia; 25925; 273 antibodies from 27 providers.
DR DNASU; 76293; -.
DR Ensembl; ENSMUST00000040522.7; ENSMUSP00000038971.7; ENSMUSG00000042436.13. [Q9D1H9-2]
DR Ensembl; ENSMUST00000064783.10; ENSMUSP00000070848.4; ENSMUSG00000042436.13. [Q9D1H9-1]
DR GeneID; 76293; -.
DR KEGG; mmu:76293; -.
DR UCSC; uc007jhm.1; mouse. [Q9D1H9-1]
DR AGR; MGI:1342276; -.
DR CTD; 4239; -.
DR MGI; MGI:1342276; Mfap4.
DR VEuPathDB; HostDB:ENSMUSG00000042436; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000154615; -.
DR HOGENOM; CLU_038628_6_0_1; -.
DR InParanoid; Q9D1H9; -.
DR OMA; PPCAPQI; -.
DR OrthoDB; 3134470at2759; -.
DR PhylomeDB; Q9D1H9; -.
DR TreeFam; TF336658; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 76293; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Mfap4; mouse.
DR PRO; PR:Q9D1H9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D1H9; Protein.
DR Bgee; ENSMUSG00000042436; Expressed in left lung lobe and 191 other cell types or tissues.
DR Genevisible; Q9D1H9; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0071953; C:elastic fiber; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001527; C:microfibril; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071493; P:cellular response to UV-B; ISO:MGI.
DR GO; GO:0048251; P:elastic fiber assembly; ISO:MGI.
DR GO; GO:0010712; P:regulation of collagen metabolic process; ISO:MGI.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:0009650; P:UV protection; ISO:MGI.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 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 NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR PANTHER; PTHR19143:SF225; MICROFIBRIL-ASSOCIATED GLYCOPROTEIN 4; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..257
FT /note="Microfibril-associated glycoprotein 4"
FT /id="PRO_0000009135"
FT DOMAIN 34..257
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT MOTIF 28..30
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT VAR_SEQ 115
FT /note="G -> GKVGPWGGGCPSAKSLLTGCHPSLG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_013482"
SQ SEQUENCE 257 AA; 28938 MW; A1E80B9671399766 CRC64;
MKALPALPLM LMLLSMPPPC APQASGIRGD ALEKSCLQQP LDCDDIYAQG YQEDGVYLIY
PYGPSVPVPV FCDMTTEGGK WTVFQKRFNG SVSFFRGWSD YKLGFGRADG EYWLGLQNLH
LLTLKQKYEL RVDLEDFENN TAYAKYIDFS ISPNAISAEE DGYTLYVAGF EDGGAGDSLS
YHSGQKFSTF DRDQDLFVQN CAALSSGAFW FRSCHFANLN GFYLGGSHLS YANGINWAQW
KGFYYSLKRT EMKIRRA
//
