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MFAP5_MOUSE
ID   MFAP5_MOUSE             Reviewed;         164 AA.
AC   Q9QZJ6;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Microfibrillar-associated protein 5;
DE            Short=MFAP-5;
DE   AltName: Full=Microfibril-associated glycoprotein 2;
DE            Short=MAGP-2;
DE   Flags: Precursor;
GN   Name=Mfap5; Synonyms=Magp2;
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].
RX   PubMed=10723723; DOI=10.1007/s003350010036;
RA   Frankfater C., Maus E., Gaal K., Segade F., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Shipley J.M.;
RT   "Organization of the mouse microfibril-associated glycoprotein-2 (MAGP-2)
RT   gene.";
RL   Mamm. Genome 11:191-195(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TGFB2 AND BMP2.
RX   PubMed=23963447; DOI=10.1074/jbc.m113.497727;
RA   Combs M.D., Knutsen R.H., Broekelmann T.J., Toennies H.M., Brett T.J.,
RA   Miller C.A., Kober D.L., Craft C.S., Atkinson J.J., Shipley J.M.,
RA   Trask B.C., Mecham R.P.;
RT   "Microfibril-associated glycoprotein 2 (MAGP2) loss of function has
RT   pleiotropic effects in vivo.";
RL   J. Biol. Chem. 288:28869-28880(2013).
CC   -!- FUNCTION: May play a role in hematopoiesis. In the cardiovascular
CC       system, could regulate growth factors or participate in cell signaling
CC       in maintaining large vessel integrity (PubMed:23963447). Component of
CC       the elastin-associated microfibrils (By similarity).
CC       {ECO:0000250|UniProtKB:Q13361, ECO:0000269|PubMed:23963447}.
CC   -!- SUBUNIT: Interacts with TGFB2 (PubMed:23963447). Interacts with BMP2.
CC       Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q28022, ECO:0000269|PubMed:23963447}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: Forms intermolecular disulfide bonds either with other MAGP-2
CC       molecules or with other components of the microfibrils. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice appear normal by several measures, are
CC       fertile, and have a normal life span, but are neutropenic.
CC       {ECO:0000269|PubMed:23963447}.
CC   -!- SIMILARITY: Belongs to the MFAP family. {ECO:0000305}.
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DR   EMBL; AF180805; AAD53950.1; -; mRNA.
DR   EMBL; AK011458; BAB27631.1; -; mRNA.
DR   EMBL; AK003479; BAB22810.1; -; mRNA.
DR   EMBL; BC025131; AAH25131.1; -; mRNA.
DR   CCDS; CCDS20496.1; -.
DR   RefSeq; NP_056591.1; NM_015776.2.
DR   AlphaFoldDB; Q9QZJ6; -.
DR   IntAct; Q9QZJ6; 1.
DR   STRING; 10090.ENSMUSP00000122863; -.
DR   GlyGen; Q9QZJ6; 1 site.
DR   iPTMnet; Q9QZJ6; -.
DR   PhosphoSitePlus; Q9QZJ6; -.
DR   MaxQB; Q9QZJ6; -.
DR   PaxDb; Q9QZJ6; -.
DR   PRIDE; Q9QZJ6; -.
DR   ProteomicsDB; 295562; -.
DR   Antibodypedia; 2040; 223 antibodies from 32 providers.
DR   DNASU; 50530; -.
DR   Ensembl; ENSMUST00000148517; ENSMUSP00000122863; ENSMUSG00000030116.
DR   GeneID; 50530; -.
DR   KEGG; mmu:50530; -.
DR   UCSC; uc009dpi.1; mouse.
DR   CTD; 8076; -.
DR   MGI; MGI:1354387; Mfap5.
DR   VEuPathDB; HostDB:ENSMUSG00000030116; -.
DR   eggNOG; ENOG502S4DY; Eukaryota.
DR   GeneTree; ENSGT00390000017736; -.
DR   InParanoid; Q9QZJ6; -.
DR   OMA; LXCRDEK; -.
DR   OrthoDB; 1427454at2759; -.
DR   PhylomeDB; Q9QZJ6; -.
DR   TreeFam; TF333418; -.
DR   Reactome; R-MMU-1566948; Elastic fibre formation.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   BioGRID-ORCS; 50530; 7 hits in 75 CRISPR screens.
DR   ChiTaRS; Mfap5; mouse.
DR   PRO; PR:Q9QZJ6; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QZJ6; protein.
DR   Bgee; ENSMUSG00000030116; Expressed in decidua and 158 other tissues.
DR   ExpressionAtlas; Q9QZJ6; baseline and differential.
DR   Genevisible; Q9QZJ6; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0001527; C:microfibril; ISS:UniProtKB.
DR   GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; TAS:MGI.
DR   GO; GO:0060216; P:definitive hemopoiesis; IMP:UniProtKB.
DR   GO; GO:0048048; P:embryonic eye morphogenesis; IBA:GO_Central.
DR   GO; GO:0097435; P:supramolecular fiber organization; IDA:MGI.
DR   InterPro; IPR008673; MAGP.
DR   PANTHER; PTHR16485; PTHR16485; 1.
DR   Pfam; PF05507; MAGP; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..164
FT                   /note="Microfibrillar-associated protein 5"
FT                   /id="PRO_0000018686"
FT   MOTIF           30..32
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        15
FT                   /note="I -> V (in Ref. 3; AAH25131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="G -> D (in Ref. 3; AAH25131)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   164 AA;  18538 MW;  8DDB1EECADE52E13 CRC64;
     MLFLGQKALL LVLAISIPSD WLPLGVSGQR GDDVPETFTD DPNLVNDPST DDTALADITP
     STDDLAGDKN ATAECRDEKF ACTRLYSVHR PVRQCVHQSC FTSLRRMYII NNEICSRLVC
     KEHEAMKDEL CRQMAGLPPR RLRRSNYFRL PPCENMNLQR PDGL
 
 
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