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MMRN1_MOUSE
ID   MMRN1_MOUSE             Reviewed;        1210 AA.
AC   B2RPV6; Q6KDN2; Q80VQ7; Q9D5S2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Multimerin-1 {ECO:0000312|EMBL:AAI37624.1};
DE   Flags: Precursor;
GN   Name=Mmrn1 {ECO:0000312|EMBL:AAI37624.1, ECO:0000312|MGI:MGI:1918195};
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] {ECO:0000305, ECO:0000312|EMBL:BAB29654.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29654.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB29654.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAI37624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NMRI {ECO:0000312|EMBL:AAH46425.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI37624.1}, and
RC   Mammary tumor {ECO:0000312|EMBL:AAH46425.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:CAE52464.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 930-1210 (ISOFORM 1).
RC   STRAIN=ICR {ECO:0000312|EMBL:CAE52464.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:CAE52464.1};
RX   PubMed=15177571; DOI=10.1016/j.ygeno.2003.12.014;
RA   Specht C.G., Schoepfer R.;
RT   "Deletion of multimerin-1 in alpha-synuclein-deficient mice.";
RL   Genomics 83:1176-1178(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Carrier protein for platelet (but not plasma) factor V/Va.
CC       Plays a role in the storage and stabilization of factor V in platelets.
CC       Upon release following platelet activation, may limit platelet and
CC       plasma factor Va-dependent thrombin generation. Ligand for integrin
CC       alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets,
CC       and may function as an extracellular matrix or adhesive protein (By
CC       similarity). {ECO:0000250|UniProtKB:Q13201}.
CC   -!- SUBUNIT: Multimeric. Composed of varying sized, disulfide-linked
CC       multimers, the smallest of which is a homotrimer. Proteolysis of the
CC       promultimerin in the N-terminal region, leads to the mature p155 form
CC       that is stored in platelets. Interacts with factor V/Va (By
CC       similarity). {ECO:0000250|UniProtKB:Q13201}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:15177571, ECO:0000269|PubMed:15489334};
CC         IsoId=B2RPV6-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:16141072};
CC         IsoId=B2RPV6-2; Sequence=VSP_053049;
CC   -!- PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q13201}.
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DR   EMBL; AK014984; BAB29654.1; -; mRNA.
DR   EMBL; BC046425; AAH46425.1; -; mRNA.
DR   EMBL; BC137623; AAI37624.1; -; mRNA.
DR   EMBL; AJ586616; CAE52464.1; -; mRNA.
DR   CCDS; CCDS51799.1; -. [B2RPV6-1]
DR   RefSeq; NP_001156979.1; NM_001163507.1.
DR   RefSeq; NP_081889.1; NM_027613.1.
DR   AlphaFoldDB; B2RPV6; -.
DR   SMR; B2RPV6; -.
DR   BioGRID; 214362; 2.
DR   ComplexPortal; CPX-447; Multimerin-1 complex.
DR   STRING; 10090.ENSMUSP00000119609; -.
DR   GlyGen; B2RPV6; 16 sites.
DR   iPTMnet; B2RPV6; -.
DR   PhosphoSitePlus; B2RPV6; -.
DR   MaxQB; B2RPV6; -.
DR   PaxDb; B2RPV6; -.
DR   PeptideAtlas; B2RPV6; -.
DR   PRIDE; B2RPV6; -.
DR   ProteomicsDB; 291374; -. [B2RPV6-1]
DR   ProteomicsDB; 291375; -. [B2RPV6-2]
DR   GeneID; 70945; -.
DR   KEGG; mmu:70945; -.
DR   UCSC; uc009cdq.1; mouse. [B2RPV6-2]
DR   CTD; 22915; -.
DR   MGI; MGI:1918195; Mmrn1.
DR   eggNOG; ENOG502QTYP; Eukaryota.
DR   InParanoid; B2RPV6; -.
DR   OrthoDB; 1205089at2759; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   BioGRID-ORCS; 70945; 4 hits in 73 CRISPR screens.
DR   PRO; PR:B2RPV6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; B2RPV6; protein.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:1990972; C:multimerin complex; ISO:MGI.
DR   GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
DR   GO; GO:0061045; P:negative regulation of wound healing; IDA:ComplexPortal.
DR   GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:ComplexPortal.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR033188; MMRN1.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427:SF3; PTHR15427:SF3; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07546; EMI; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1210
FT                   /note="Multimerin-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000367039"
FT   DOMAIN          192..267
FT                   /note="EMI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DOMAIN          1023..1059
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1078..1210
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          57..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..338
FT                   /evidence="ECO:0000255"
FT   COILED          564..690
FT                   /evidence="ECO:0000255"
FT   COILED          809..846
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        143..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        525
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        765
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        810
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        822
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        903
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        915
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        963
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1000
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..257
FT                   /evidence="ECO:0000255"
FT   DISULFID        222..230
FT                   /evidence="ECO:0000255"
FT   DISULFID        256..265
FT                   /evidence="ECO:0000255"
FT   DISULFID        1027..1038
FT                   /evidence="ECO:0000255"
FT   DISULFID        1032..1047
FT                   /evidence="ECO:0000255"
FT   DISULFID        1049..1058
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         194..1210
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_053049"
FT   CONFLICT        41
FT                   /note="H -> P (in Ref. 1; BAB29654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="E -> D (in Ref. 1; BAB29654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="H -> S (in Ref. 1; BAB29654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="P -> S (in Ref. 1; BAB29654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="L -> M (in Ref. 1; BAB29654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        935
FT                   /note="L -> V (in Ref. 1; AAI37624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1210 AA;  136106 MW;  971CBB31F6827DD5 CRC64;
     MLGLKFLVLL SILWGRVFRL TNTQHSWTAP KDEDASLTPN HASASVSEIL SLQVLSATQN
     PSTQGPAAAE RSSEDDVLLQ STSQPSETST PPEGRHQTPL EKTGTAVVSL PLSLQDKPSI
     KPSTGAGTVM LANATLKFLQ SFSRKSDQQE VSTKSAGDMG NRSARETHLR RSDNSRNQRP
     SYQKPSFETT RGKNWCAHVH TKLSPTVILD TGSHLPSGRG SCGWYSSGLC SRRSQKTSNA
     VYRMQHKIVT SLEWRCCPGY IGPNCQLKVE EQQQLAHSNQ AESHTAVDQG RAQQQKQDCG
     DPAMIQKLAE QLSQQERKLS LLQKKVDNAS LVADDMRNAY LSLEGKVGED NSRQFQSFLK
     ALKSKSIEDL LKNIVKEQFK VFQDDMQETT AQIFKTVSSL SEDLESTRQA VLQVNQSFVS
     STAQKDFAFM QENQPTWKDI TDLKNSIMNI RQEMALTCEK PVKELEAKQA HLEGALRQEH
     SQIVLYHQSL NETLSKMQEA HIQLLSVLQV SGTENVATEE SLNSNVTKYI SVLQETASKQ
     GLMLLQMLSD LHVQESKISN LTILLEMEKE SARGECEEML SKCRHDFKFQ LKDTEENLHV
     LNQTLSEVIF PMDIKVDKMS EQLNDLTYDM EILQPLLEQR SSLQHQVIHK PKEATVTRRE
     LQNLIGAINQ LNVLTKELTK RHNLLRNEVQ SRGEAFERRI SEHALETEDG LNKTMTVINN
     AIDFVQDNYV LKETLSAMTY NPKVCECNQN MDNILTFVSE FQHLNDSIQT LVNNKEKYNF
     ILQIAKALTA IPKDEKLNQL NFQNIYQLFN ETTSQVNKCQ QNMSHLEENM LSVTKTAKEF
     ETRLQGIESK VTKTLIPYYI SFKKGGILSN ERDVDLQLKV LNTRFKALEA KSIHLSVSFS
     LLNKTVRELS MACRNASTGT CGQNALIPRW TKGSLPGSQS SQKSLTELVE SIVEIKTQAA
     LSNLTWNVDR LLSDTLANIV KPQKQIKLQK KPNTLKKTVN MTTILIGRTQ RNTDTIIHPV
     AQEHSSCSSF PCQNGGTCIS GRSNFICACR HPFMGDTCTV KIKEDDAVAP DFSKGSYRYA
     PMVAFFVSHT HGMTAPGPIL FNDLSVNYGA SYNPRTGKFR IPYLGVYIFK YTIESFSAHI
     SGFFVVDGVD KLRFESENAD NEIHCDRVLT GDALFELNYG QEVWLRLVKG TIPIKYPPVT
     TFSGYLLYRT
 
 
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