ID   ECM2_HUMAN              Reviewed;         699 AA.
AC   O94769; B2R730; E2PU11; Q5T9F2; Q7Z3D0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Extracellular matrix protein 2;
DE   AltName: Full=Matrix glycoprotein SC1/ECM2;
DE   Flags: Precursor;
GN   Name=ECM2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=9790758; DOI=10.1006/geno.1998.5455;
RA   Nishiu J., Tanaka T., Nakamura Y.;
RT   "Identification of a novel gene (ECM2) encoding a putative extracellular
RT   matrix protein expressed predominantly in adipose and female-specific
RT   tissues and its chromosomal localization to 9q22.3.";
RL   Genomics 52:378-381(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-56.
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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).
CC   -!- FUNCTION: Promotes matrix assembly and cell adhesiveness.
CC       {ECO:0000250|UniProtKB:Q5FW85}.
CC   -!- SUBUNIT: Interacts with numerous extracellular matrix proteins (By
CC       similarity). Interacts with MSL1 and RASSF1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q5FW85}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q5FW85}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O94769-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O94769-2; Sequence=VSP_039114, VSP_039115;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in adipose tissue as well
CC       as female-specific organs such as mammary gland, ovary, and uterus.
CC       {ECO:0000269|PubMed:9790758}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD97940.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB011792; BAA33958.1; -; mRNA.
DR   EMBL; AK312820; BAG35677.1; -; mRNA.
DR   EMBL; BX537976; CAD97940.1; ALT_INIT; mRNA.
DR   EMBL; AL137848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62824.1; -; Genomic_DNA.
DR   EMBL; BC107493; AAI07494.1; -; mRNA.
DR   CCDS; CCDS56578.1; -. [O94769-2]
DR   CCDS; CCDS6698.1; -. [O94769-1]
DR   RefSeq; NP_001184224.1; NM_001197295.1.
DR   RefSeq; NP_001184225.1; NM_001197296.1. [O94769-2]
DR   RefSeq; NP_001384.1; NM_001393.3. [O94769-1]
DR   AlphaFoldDB; O94769; -.
DR   SMR; O94769; -.
DR   BioGRID; 108175; 1.
DR   IntAct; O94769; 1.
DR   STRING; 9606.ENSP00000344758; -.
DR   GlyConnect; 1229; 3 N-Linked glycans (1 site).
DR   GlyCosmos; O94769; 5 sites, 6 glycans.
DR   GlyGen; O94769; 6 sites, 3 N-linked glycans (1 site), 3 O-linked glycans (2 sites).
DR   iPTMnet; O94769; -.
DR   PhosphoSitePlus; O94769; -.
DR   BioMuta; ECM2; -.
DR   jPOST; O94769; -.
DR   MassIVE; O94769; -.
DR   PaxDb; 9606-ENSP00000344758; -.
DR   PeptideAtlas; O94769; -.
DR   ProteomicsDB; 50433; -. [O94769-1]
DR   ProteomicsDB; 50434; -. [O94769-2]
DR   Antibodypedia; 43750; 33 antibodies from 15 providers.
DR   DNASU; 1842; -.
DR   Ensembl; ENST00000344604.10; ENSP00000344758.5; ENSG00000106823.13. [O94769-1]
DR   Ensembl; ENST00000444490.6; ENSP00000393971.2; ENSG00000106823.13. [O94769-2]
DR   Ensembl; ENST00000707290.1; ENSP00000516826.1; ENSG00000291357.1. [O94769-2]
DR   Ensembl; ENST00000707291.1; ENSP00000516827.1; ENSG00000291357.1. [O94769-1]
DR   GeneID; 1842; -.
DR   KEGG; hsa:1842; -.
DR   MANE-Select; ENST00000344604.10; ENSP00000344758.5; NM_001393.4; NP_001384.1.
DR   UCSC; uc004asf.5; human. [O94769-1]
DR   AGR; HGNC:3154; -.
DR   CTD; 1842; -.
DR   DisGeNET; 1842; -.
DR   GeneCards; ECM2; -.
DR   HGNC; HGNC:3154; ECM2.
DR   HPA; ENSG00000106823; Tissue enhanced (adipose tissue, ovary).
DR   MIM; 603479; gene.
DR   neXtProt; NX_O94769; -.
DR   OpenTargets; ENSG00000106823; -.
DR   PharmGKB; PA27599; -.
DR   VEuPathDB; HostDB:ENSG00000106823; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000159941; -.
DR   HOGENOM; CLU_000288_186_2_1; -.
DR   InParanoid; O94769; -.
DR   OMA; MTMYNRA; -.
DR   OrthoDB; 5361311at2759; -.
DR   PhylomeDB; O94769; -.
DR   TreeFam; TF330031; -.
DR   PathwayCommons; O94769; -.
DR   SignaLink; O94769; -.
DR   BioGRID-ORCS; 1842; 14 hits in 1149 CRISPR screens.
DR   ChiTaRS; ECM2; human.
DR   GeneWiki; ECM2; -.
DR   GenomeRNAi; 1842; -.
DR   Pharos; O94769; Tdark.
DR   PRO; PR:O94769; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; O94769; Protein.
DR   Bgee; ENSG00000106823; Expressed in calcaneal tendon and 194 other cell types or tissues.
DR   ExpressionAtlas; O94769; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR   GO; GO:0070052; F:collagen V binding; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR   GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; SM00364; LRR_BAC; 4.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 12.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; O94769; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Extracellular matrix; Glycoprotein;
KW   Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..699
FT                   /note="Extracellular matrix protein 2"
FT                   /id="PRO_0000032731"
FT   DOMAIN          101..158
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          307..344
FT                   /note="LRRNT"
FT   REPEAT          368..388
FT                   /note="LRR 1"
FT   REPEAT          394..415
FT                   /note="LRR 2"
FT   REPEAT          416..436
FT                   /note="LRR 3"
FT   REPEAT          439..459
FT                   /note="LRR 4"
FT   REPEAT          465..484
FT                   /note="LRR 5"
FT   REPEAT          486..507
FT                   /note="LRR 6"
FT   REPEAT          510..530
FT                   /note="LRR 7"
FT   REPEAT          536..557
FT                   /note="LRR 8"
FT   REPEAT          558..578
FT                   /note="LRR 9"
FT   REPEAT          582..602
FT                   /note="LRR 10"
FT   REPEAT          609..630
FT                   /note="LRR 11"
FT   REPEAT          632..653
FT                   /note="LRR 12"
FT   REPEAT          661..684
FT                   /note="LRR 13"
FT   REGION          176..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           294..296
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        244..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         161..182
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_039114"
FT   VAR_SEQ         645..699
FT                   /note="NILPEEICNAEEDDDSNLEHLHLENNYIKIREIPSYTFSCIRSYSSIVLKPQ
FT                   NIK -> CVSDAVLETVTNRSDVAFPLW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_039115"
FT   VARIANT         56
FT                   /note="Q -> P (in dbSNP:rs10120210)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_024646"
FT   VARIANT         109
FT                   /note="T -> S (in dbSNP:rs35496743)"
FT                   /id="VAR_052010"
FT   VARIANT         204
FT                   /note="R -> Q (in dbSNP:rs34758505)"
FT                   /id="VAR_052011"
SQ   SEQUENCE   699 AA;  79789 MW;  E44E76A40A5C2742 CRC64;
     MKIAVLFCFF LLIIFQTDFG KNEEIPRKQR RKIYHRRLRK SSTSHKHRSN RQLGIQQTTV
     FTPVARLPIV NFDYSMEEKF ESFSSFPGVE SSYNVLPGKK GHCLVKGITM YNKAVWSPEP
     CTTCLCSDGR VLCDETMCHP QRCPQTVIPE GECCPVCSAT VSYSLLSGIA LNDRNEFSGD
     SSEQREPTNL LHKQLPPPQV GMDRIVRKEA LQSEEDEEVK EEDTEQKRET PESRNQGQLY
     SEGDSRGGDR KQRPGEERRL AHQQQRQGRE EEEDEEEEGE EGEEDEEDEE DPVRGDMFRM
     PSRSPLPAPP RGTLRLPSGC SLSYRTISCI NAMLTQIPPL TAPQITSLEL TGNSIASIPD
     EAFNGLPNLE RLDLSKNNIT SSGIGPKAFK LLKKLMRLNM DGNNLIQIPS QLPSTLEELK
     VNENNLQAID EESLSDLNQL VTLELEGNNL SEANVNPLAF KPLKSLAYLR LGKNKFRIIP
     QGLPGSIEEL YLENNQIEEI TEICFNHTRK INVIVLRYNK IEENRIAPLA WINQENLESI
     DLSYNKLYHV PSYLPKSLLH LVLLGNQIER IPGYVFGHME PGLEYLYLSF NKLADDGMDR
     VSFYGAYHSL RELFLDHNDL KSIPPGIQEM KALHFLRLNN NKIRNILPEE ICNAEEDDDS
     NLEHLHLENN YIKIREIPSY TFSCIRSYSS IVLKPQNIK
//