ECM2_MOUSE
ID ECM2_MOUSE Reviewed; 670 AA.
AC Q5FW85;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Extracellular matrix protein 2;
DE AltName: Full=Tenonectin;
DE Flags: Precursor;
GN Name=Ecm2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Medulla oblongata;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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]
RP INTERACTION WITH MSL1 AND RASSF1.
RX PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA Modyanov N.N., Pestov N.B.;
RT "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- FUNCTION: Promotes matrix assembly and cell adhesiveness.
CC {ECO:0000269|PubMed:18757743}.
CC -!- SUBUNIT: Interacts with numerous extracellular matrix proteins
CC (PubMed:18757743). Interacts with isoform 1 of MSL1 (PubMed:17335777).
CC Interacts with isoform 3 of RASSF1 (PubMed:17335777).
CC {ECO:0000269|PubMed:17335777, ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}.
CC -!- DEVELOPMENTAL STAGE: At 16.5 dpc, present in periosteum of ribs. At P0,
CC present in tendons connecting the scapula and humerus to muscles (at
CC protein level). {ECO:0000269|PubMed:18757743}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000305}.
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DR EMBL; AK038812; BAE20541.1; -; mRNA.
DR EMBL; AK040995; BAE20587.1; -; mRNA.
DR EMBL; AK134746; BAE22265.1; -; mRNA.
DR EMBL; BC065151; AAH65151.1; -; mRNA.
DR EMBL; BC089559; AAH89559.1; -; mRNA.
DR CCDS; CCDS26502.1; -.
DR RefSeq; NP_001012324.1; NM_001012324.2.
DR AlphaFoldDB; Q5FW85; -.
DR SMR; Q5FW85; -.
DR STRING; 10090.ENSMUSP00000060402; -.
DR GlyGen; Q5FW85; 3 sites.
DR iPTMnet; Q5FW85; -.
DR PhosphoSitePlus; Q5FW85; -.
DR MaxQB; Q5FW85; -.
DR PaxDb; Q5FW85; -.
DR PRIDE; Q5FW85; -.
DR ProteomicsDB; 277628; -.
DR Antibodypedia; 43750; 32 antibodies from 15 providers.
DR Ensembl; ENSMUST00000051504; ENSMUSP00000060402; ENSMUSG00000043631.
DR GeneID; 407800; -.
DR KEGG; mmu:407800; -.
DR UCSC; uc007qjl.1; mouse.
DR CTD; 1842; -.
DR MGI; MGI:3039578; Ecm2.
DR VEuPathDB; HostDB:ENSMUSG00000043631; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159941; -.
DR HOGENOM; CLU_000288_186_2_1; -.
DR InParanoid; Q5FW85; -.
DR OMA; KQRRKMY; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q5FW85; -.
DR TreeFam; TF330031; -.
DR BioGRID-ORCS; 407800; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Ecm2; mouse.
DR PRO; PR:Q5FW85; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q5FW85; protein.
DR Bgee; ENSMUSG00000043631; Expressed in esophagus and 96 other tissues.
DR Genevisible; Q5FW85; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0070052; F:collagen V binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR043184; ECM2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46544; PTHR46544; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..670
FT /note="Extracellular matrix protein 2"
FT /id="PRO_0000287728"
FT DOMAIN 96..153
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 278..315
FT /note="LRRNT"
FT REPEAT 339..359
FT /note="LRR 1"
FT REPEAT 365..386
FT /note="LRR 2"
FT REPEAT 387..407
FT /note="LRR 3"
FT REPEAT 410..430
FT /note="LRR 4"
FT REPEAT 436..456
FT /note="LRR 5"
FT REPEAT 457..478
FT /note="LRR 6"
FT REPEAT 481..501
FT /note="LRR 7"
FT REPEAT 507..528
FT /note="LRR 8"
FT REPEAT 529..549
FT /note="LRR 9"
FT REPEAT 553..573
FT /note="LRR 10"
FT REPEAT 580..601
FT /note="LRR 11"
FT REPEAT 603..624
FT /note="LRR 12"
FT REPEAT 632..655
FT /note="LRR 13"
FT REGION 185..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..268
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 185..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 76676 MW; 025BE9522417F5E3 CRC64;
MKLAVLFCFI LLIVLQTDCE RGTRRQRRRM HQRRLRKSSS FHLRANRQLE VQQTTAAPDA
RLPTANSDYS VEENIESLLS NLGVESSYSV LPGKKGYCFV KGMIMYNKAV WSPEPCTTCL
CSNGRVLCDE TECHPKACPY TIKPEGECCP ICSDAEQESI NKLHKQVPPP QMEMDQVAIK
EALQSEEDEE IAEGHKEHKK ETSVPTKIHG DGERTERKLR PEKEGRSAHQ PLYHGRREEE
ESKEETEREG EEEEEEEEEE EEDAIRGDVF RMSSRVIPGT PRGRPRLPRS CSLSYRTISC
VHADFTEIPP ITAPEVTNLE LVGNSIISIP DEAFNGLPNL ERLDLSRNNI TSSGIGPKAF
KSLKKLMRLN MDGNNLVHIP SDLPSTLEEL KINDNNLQAI DEKSLSDLNQ LVTLELEGNN
LSEINVDPLA FQSLESLSYL RLGRNKFRII PQGLPASTEE LYLENNQIEE ITEICFNHTR
KITMIILRYN KIEESRIAPL AWINQENLES IDLSYNKLYH VPSYLPKSLL HLVLIGNQID
RIPGYVFGHM QPGLEYLYLS FNRLSDDGVD LVSFYGAYHS LRELFLDHND FKSIPPGIQD
MKALHFLRLN NNKIRNIHPE QICNAEEDED SALEHLHLEN NYIRTREISS YAFSCIRLYS
SIVLKPQHIK
