ID   ECM2_BOVIN              Reviewed;         680 AA.
AC   Q3MHH9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Extracellular matrix protein 2;
DE   Flags: Precursor;
GN   Name=ECM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
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DR   EMBL; BC105232; AAI05233.1; -; mRNA.
DR   RefSeq; NP_001029769.1; NM_001034597.1.
DR   AlphaFoldDB; Q3MHH9; -.
DR   SMR; Q3MHH9; -.
DR   STRING; 9913.ENSBTAP00000015726; -.
DR   PaxDb; Q3MHH9; -.
DR   PRIDE; Q3MHH9; -.
DR   GeneID; 533916; -.
DR   KEGG; bta:533916; -.
DR   CTD; 1842; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q3MHH9; -.
DR   OrthoDB; 826997at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0070052; F:collagen V binding; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
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; -; 3.
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; 4.
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   2: Evidence at transcript level;
KW   Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..680
FT                   /note="Extracellular matrix protein 2"
FT                   /id="PRO_0000287727"
FT   DOMAIN          100..157
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          288..325
FT                   /note="LRRNT"
FT   REPEAT          349..369
FT                   /note="LRR 1"
FT   REPEAT          375..396
FT                   /note="LRR 2"
FT   REPEAT          397..417
FT                   /note="LRR 3"
FT   REPEAT          420..440
FT                   /note="LRR 4"
FT   REPEAT          446..466
FT                   /note="LRR 5"
FT   REPEAT          467..488
FT                   /note="LRR 6"
FT   REPEAT          491..511
FT                   /note="LRR 7"
FT   REPEAT          517..538
FT                   /note="LRR 8"
FT   REPEAT          539..559
FT                   /note="LRR 9"
FT   REPEAT          563..583
FT                   /note="LRR 10"
FT   REPEAT          590..611
FT                   /note="LRR 11"
FT   REPEAT          613..634
FT                   /note="LRR 12"
FT   REPEAT          642..665
FT                   /note="LRR 13"
FT   REGION          189..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           275..277
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        199..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..273
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   680 AA;  78062 MW;  19D971D3301540EF CRC64;
     MKFSSLYCFL LLLIFQTDFG QNEETSRRQR RKMYHRRLRK SSLSTHRSVR QPGIQQMKTV
     TPAAKLPIIN LDYSIEENFE SFLSVPGVES SYNVLPGKKG HCLANGMIMY NKAVWSPEPC
     TTCLCLNGKV LCDETKCHPQ MCPQTIIPEG ECCPVCSNTE QREPTNLPHK QQSPPWEEMN
     RALRKEELQL EEDEEEVKQD ENREQKKKTF RPGDWGRPIN EGQSREGKAQ RPEEEGRQAH
     QHRNPARENE EDDDEEEEDD DDEEEDDDDE DETIRGDTFR MPPRLPIPAT PRGIPSLPSM
     CSLSYKTISC ISADLTQIPP LTAPEITSLE LIDNSITSIP DEAFNGLPNL ERLDLSKNNI
     TSSGIGPKAF KFLKNLMRLN MDGNNLVTIP SELPSTLEEL KINENKLQVI DEESLSDLNQ
     LVTLELEGNN LSETNVNSLA FKPLKSLSYL RLGRNKFRII PQGLPASIEE LYLENNQIEE
     ITEISFNHTR KINVIGLRYN KIEENRIAPL AWINQENLES IDLSYNKLYH VPSYLPKSLV
     HLVLIGNQIE RIPGYVFGHM EPGLEYLYLS FNKLVDDGID RVSFYGAYHS LRELFLDHNE
     LKSIPPGVQE MKALHFLRLN NNKIRNILPE QICNAEEDDD SNLQHLHLEN NYIKTREIPS
     YAFSCIRSYS SIVLKPQNIK