ECM2_HUMAN
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 03-AUG-2022, entry version 173.
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 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; O94769; -.
DR PeptideAtlas; O94769; -.
DR PRIDE; O94769; -.
DR ProteomicsDB; 50433; -. [O94769-1]
DR ProteomicsDB; 50434; -. [O94769-2]
DR Antibodypedia; 43750; 32 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 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 CTD; 1842; -.
DR DisGeNET; 1842; -.
DR GeneCards; ECM2; -.
DR HGNC; HGNC:3154; ECM2.
DR HPA; ENSG00000106823; Tissue enhanced (adipose).
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; KQRRKMY; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O94769; -.
DR TreeFam; TF330031; -.
DR PathwayCommons; O94769; -.
DR SignaLink; O94769; -.
DR BioGRID-ORCS; 1842; 13 hits in 1068 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 192 other tissues.
DR ExpressionAtlas; O94769; baseline and differential.
DR Genevisible; O94769; HS.
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; 3.80.10.10; -; 4.
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; 12.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51450; LRR; 12.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
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
