MMRN2_MOUSE
ID MMRN2_MOUSE Reviewed; 943 AA.
AC A6H6E2; Q8BJX4; Q8K1Z7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Multimerin-2 {ECO:0000312|EMBL:AAI45846.1};
DE Flags: Precursor;
GN Name=Mmrn2 {ECO:0000312|EMBL:AAI45846.1, ECO:0000312|MGI:MGI:2385618};
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:BAC37291.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37291.1};
RC TISSUE=Muellerian duct {ECO:0000312|EMBL:BAC37291.1};
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:0000312|EMBL:EDL24879.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI45846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH34871.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH34871.1}, and
RC Thymus {ECO:0000312|EMBL:AAI45846.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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: Inhibits endothelial cells motility and acts as a negative
CC regulator of angiogenesis; it down-regulates KDR activation by binding
CC VEGFA. {ECO:0000250}.
CC -!- SUBUNIT: Heteromer of p110, p125, p140 and p200 subunits; disulfide-
CC linked. Interacts with VEGFA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9H8L6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=A6H6E2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=A6H6E2-2; Sequence=VSP_053050;
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9H8L6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37291.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK078470; BAC37291.1; ALT_FRAME; mRNA.
DR EMBL; CH466573; EDL24879.1; -; Genomic_DNA.
DR EMBL; BC034871; AAH34871.1; -; mRNA.
DR EMBL; BC145845; AAI45846.1; -; mRNA.
DR CCDS; CCDS36876.1; -. [A6H6E2-1]
DR RefSeq; NP_694767.3; NM_153127.3. [A6H6E2-1]
DR AlphaFoldDB; A6H6E2; -.
DR SMR; A6H6E2; -.
DR BioGRID; 222862; 4.
DR ComplexPortal; CPX-451; Multimerin-2 complex.
DR STRING; 10090.ENSMUSP00000107539; -.
DR GlyConnect; 2515; 1 N-Linked glycan (1 site).
DR GlyGen; A6H6E2; 12 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; A6H6E2; -.
DR CPTAC; non-CPTAC-3482; -.
DR MaxQB; A6H6E2; -.
DR PaxDb; A6H6E2; -.
DR PeptideAtlas; A6H6E2; -.
DR PRIDE; A6H6E2; -.
DR ProteomicsDB; 290266; -. [A6H6E2-1]
DR ProteomicsDB; 290267; -. [A6H6E2-2]
DR Antibodypedia; 16004; 102 antibodies from 24 providers.
DR Ensembl; ENSMUST00000111908; ENSMUSP00000107539; ENSMUSG00000041445. [A6H6E2-1]
DR GeneID; 105450; -.
DR KEGG; mmu:105450; -.
DR UCSC; uc007tav.1; mouse. [A6H6E2-1]
DR CTD; 79812; -.
DR MGI; MGI:2385618; Mmrn2.
DR VEuPathDB; HostDB:ENSMUSG00000041445; -.
DR eggNOG; ENOG502QUTH; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_012255_1_0_1; -.
DR InParanoid; A6H6E2; -.
DR OMA; NHMSTSV; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; A6H6E2; -.
DR TreeFam; TF336041; -.
DR BioGRID-ORCS; 105450; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Mmrn2; mouse.
DR PRO; PR:A6H6E2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; A6H6E2; protein.
DR Bgee; ENSMUSG00000041445; Expressed in brain blood vessel and 216 other tissues.
DR ExpressionAtlas; A6H6E2; baseline and differential.
DR Genevisible; A6H6E2; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; TAS:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:1990972; C:multimerin complex; IC:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IC:ComplexPortal.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IDA:ComplexPortal.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ComplexPortal.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:ComplexPortal.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; ISO:MGI.
DR GO; GO:1905332; P:positive regulation of morphogenesis of an epithelium; ISO:MGI.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..943
FT /note="Multimerin-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000367040"
FT DOMAIN 54..132
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 815..943
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 391..480
FT /evidence="ECO:0000255"
FT COILED 551..580
FT /evidence="ECO:0000255"
FT COILED 688..720
FT /evidence="ECO:0000255"
FT COMPBIAS 131..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 85..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 121..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT VAR_SEQ 177..702
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053050"
FT CONFLICT 352
FT /note="S -> G (in Ref. 1; BAC37291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 943 AA; 105206 MW; 8F553278E6BC2073 CRC64;
MIPTLLLGFG VYLSWGLLGS WAQDPGTKFS HLNRPGMPEG WRLGAEDTSR DPIRRNWCPY
QKSRLVTFVA ACKTEKFLVH SQQPCPQGAP DCQGVRVMYR VAQKPVYQVQ QKVLISVDWR
CCPGFQGPDC QDHNPTANPE PTEPSGKLQE TWDSMDGFEL GHPVPEFNEI KVPQEQQENL
LQNLQNDAQS VEDGFPGSWE APPSNLTDEM TEANLTEFEF PGRTSEHLLQ PHIDAFLKAH
FSPIWKNFND SLHSLSQAIR NLSLDVEANH QAIKMIQEGT VARADFQELG AKFEAKVQQN
SQRLGQLWQD VEDQLHAQRR SVHHALSDVQ AEVSTKLKQL VKAQELPGAN GSLVMASAAA
AARPEPESLQ ARLGQLQRNL SALHMVTSQR EEELQSTLKN MDSVLKQHAE EIKELYSESD
ETFDQISKVE RQVEELLVNH TGLRELRVIL MEKSLIMEEN KEEIERQLLE LNLTLQHLHA
GHADLIKYVK DCNCQRVNSD VDVAPEGHRD VMHTLEETQV SLDEQHQLDG SSLQALQSTV
DAMSSAMDAY RGEGERARAE RARIRSQLRA LDHAVEALKT AANGTRKEIR LLHGSFTALL
EDALRHQAVL AALFGEEMID EMSEEAPRPL PLDYEQIRLA LQDAASGLQE QAIGWEDLAT
RVEALEKAAG GFVEQHPQLA EGLEPSHDSG REEEAMTLAE LEQEIRRLSS DVKQIGQCCE
ASWAASLNSS LEDLHSMLLD TQHGLRQHRQ LFHNLFQNFQ GLVASNISLD LGKLQAMLSK
KDKKQPRGPG ESRKRDKKQV VMSTDAHAKG LELWETGSPV AFYAGSSEGA TALQMVKFNT
TSINVGSSYF PEHGYFRAPK RGVYLFAVSI TFGPGPGMGQ LVFEGHHRVP VYSTEQRGGS
TATTFAMVEL QKGERAWFEL IQGSATKGSQ PGTAFGGFLM FKT
