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   27-MAR-2024, entry version 151.
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   GlyCosmos; Q5FW85; 3 sites, No reported glycans.
DR   GlyGen; Q5FW85; 3 sites.
DR   iPTMnet; Q5FW85; -.
DR   PhosphoSitePlus; Q5FW85; -.
DR   MaxQB; Q5FW85; -.
DR   PaxDb; 10090-ENSMUSP00000060402; -.
DR   ProteomicsDB; 277628; -.
DR   Antibodypedia; 43750; 33 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000051504.8; ENSMUSP00000060402.8; ENSMUSG00000043631.9.
DR   GeneID; 407800; -.
DR   KEGG; mmu:407800; -.
DR   UCSC; uc007qjl.1; mouse.
DR   AGR; MGI:3039578; -.
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; MTMYNRA; -.
DR   OrthoDB; 5361311at2759; -.
DR   PhylomeDB; Q5FW85; -.
DR   TreeFam; TF330031; -.
DR   BioGRID-ORCS; 407800; 6 hits in 76 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 97 other cell types or tissues.
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; 6.20.200.20; -; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR043184; ECM2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR46544:SF1; EXTRACELLULAR MATRIX PROTEIN 2; 1.
DR   PANTHER; PTHR46544; EXTRACELLULAR MATRIX PROTEIN 2-RELATED; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 13.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; Q5FW85; MM.
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
//