MFAP3_MOUSE
ID MFAP3_MOUSE Reviewed; 349 AA.
AC Q922T2; Q8BHK5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Microfibril-associated glycoprotein 3;
DE Flags: Precursor;
GN Name=Mfap3;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and 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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000305}.
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DR EMBL; AK042988; BAC31429.1; -; mRNA.
DR EMBL; AK076071; BAC36162.1; -; mRNA.
DR EMBL; BC006828; AAH06828.1; -; mRNA.
DR CCDS; CCDS24718.1; -.
DR RefSeq; NP_663401.2; NM_145426.2.
DR RefSeq; NP_850930.1; NM_180599.1.
DR RefSeq; XP_006532913.1; XM_006532850.2.
DR AlphaFoldDB; Q922T2; -.
DR STRING; 10090.ENSMUSP00000020830; -.
DR GlyGen; Q922T2; 4 sites.
DR iPTMnet; Q922T2; -.
DR PhosphoSitePlus; Q922T2; -.
DR SwissPalm; Q922T2; -.
DR jPOST; Q922T2; -.
DR MaxQB; Q922T2; -.
DR PaxDb; Q922T2; -.
DR PRIDE; Q922T2; -.
DR ProteomicsDB; 252542; -.
DR DNASU; 216760; -.
DR GeneID; 216760; -.
DR KEGG; mmu:216760; -.
DR UCSC; uc007izx.1; mouse.
DR CTD; 4238; -.
DR MGI; MGI:1924068; Mfap3.
DR eggNOG; ENOG502QW9J; Eukaryota.
DR InParanoid; Q922T2; -.
DR OrthoDB; 1154642at2759; -.
DR PhylomeDB; Q922T2; -.
DR TreeFam; TF333205; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 216760; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mfap3; mouse.
DR PRO; PR:Q922T2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q922T2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR039696; MFAP3-like.
DR PANTHER; PTHR14340; PTHR14340; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..349
FT /note="Microfibril-associated glycoprotein 3"
FT /id="PRO_0000014866"
FT TOPO_DOM 22..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..130
FT /note="Ig-like C2-type"
FT REGION 280..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 9
FT /note="F -> I (in Ref. 1; BAC31429/BAC36162)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="S -> G (in Ref. 1; BAC31429/BAC36162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38406 MW; A6D47FF251B9167D CRC64;
MKLHHCLSFL LVVTLVPAAL SLEDVAPLGA NQSSYNASFL PSFELSAGSY SGDDVIIVKE
GTNVSLECLL TVDQYGEVHW YNSKGQQLHS RGGKWLVSDN FLNITSVAFD DRGLYTCIIT
SPARASYSVT LRVIFTSGDM SVYYMVVCLI AFTITLILNV TRLCLMSTHL RKTEKAINEF
FRTEGAEKLQ KAFEIAKRIP IITSAKTLEL AKVTQFKTME FARYIEELAR SVPLPPLILN
CRAFVEEMFE AVRVDDPDDM GERIKERPAL DAQSGIYVIN PELGRSNSPG GDSDDGSLSE
QGQEIAVQVS VHLQSETKSI GTDSQDSSHF SPPSDPASAE GSIHHRVSI
