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
