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Database: UniProt
Entry: MMRN2_MOUSE
LinkDB: MMRN2_MOUSE
Original site: 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   24-JAN-2024, entry version 108.
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   GlyCosmos; A6H6E2; 12 sites, 1 glycan.
DR   GlyGen; A6H6E2; 13 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; A6H6E2; -.
DR   PhosphoSitePlus; A6H6E2; -.
DR   CPTAC; non-CPTAC-3482; -.
DR   MaxQB; A6H6E2; -.
DR   PaxDb; 10090-ENSMUSP00000107539; -.
DR   PeptideAtlas; A6H6E2; -.
DR   ProteomicsDB; 290266; -. [A6H6E2-1]
DR   ProteomicsDB; 290267; -. [A6H6E2-2]
DR   Antibodypedia; 16004; 123 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000111908.3; ENSMUSP00000107539.2; ENSMUSG00000041445.10. [A6H6E2-1]
DR   GeneID; 105450; -.
DR   KEGG; mmu:105450; -.
DR   UCSC; uc007tav.1; mouse. [A6H6E2-1]
DR   AGR; MGI:2385618; -.
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; 4634169at2759; -.
DR   PhylomeDB; A6H6E2; -.
DR   TreeFam; TF336041; -.
DR   BioGRID-ORCS; 105450; 4 hits in 77 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 218 other cell types or 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; ISS:ComplexPortal.
DR   GO; GO:0007155; P:cell adhesion; NAS: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   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   PANTHER; PTHR15427:SF6; MULTIMERIN-2; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF07546; EMI; 1.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 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
//
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