ID A0A6J8A7N9_MYTCO Unreviewed; 1350 AA.
AC A0A6J8A7N9;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=MCOR_4019 {ECO:0000313|EMBL:CAC5362175.1};
OS Mytilus coruscus (Sea mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=42192 {ECO:0000313|EMBL:CAC5362175.1, ECO:0000313|Proteomes:UP000507470};
RN [1] {ECO:0000313|EMBL:CAC5362175.1, ECO:0000313|Proteomes:UP000507470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wild {ECO:0000313|Proteomes:UP000507470};
RA Li R., Bekaert M.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CACVKT020000733; CAC5362175.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000507470; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 7.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000507470};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 29..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 231..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..504
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..532
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..831
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..880
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1099
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 135548 MW; 26631A43F163D352 CRC64;
MNIIQDLKLQ ITQLAHDCLI ISKEIKKTEV DLMAAVGLPD PSKGVTYDVG LEGFPAFKLD
KSAYIRKAAE TYFTDRIGKI NDFAIGITVK VFSKDGFLFA VKNIYESVIA FGVRITAAGN
GKHNVVLYYT EDHQYGQVSK AIGNFTVDNI DKDSFTKLAL KVQGDTVTLF DNCEEVGRQQ
VANRRPLQFN TGSGLYIGQG GPNFDDTSFE GVIQELKYYT NPAKAEELDC LSLDSGSGSG
GDDDEDRVKP VITLPPPTGK PGEKGEKGDT GEPGKDGKDG KDGKDGEKGE KGDVGPVGPP
GPPPSLTPPP PELLEDMMGA KGERGETGPR GEQGETGIDG FPGQKGEKGD PGTIGPEGPA
GIQGPKGDQG ERGLPGIGQV GPQGDPGLPA SVDNQVIANA ILSQMHMDPG QKGEKGETGQ
RGENGSDGND GREGIPGRDG LPGLPGEKGE KGDTVVGPEG PQGPVGQPGE TGLPGIAGVA
GPTGPMGPPG PPGPGGLITE GSGDGDAEPG LPGPPGPMGP IGPQGIQGLV GPMGVAGPKG
DPGVIGTPGI PGLPGTPGTP GVFAGNLSEM IGTPGKDGAP GLQGEPGLPG ASGPRGFDGP
VGPAGDKGDK GDSGEPGPRG QAGINGEPGV SGPIGPQGPQ GLSGSDGSVG PQGPPGLPGP
PGKGYDGPIR GDTGLVDIEG SGDCGCEPGL PGIQGPSGPV GKQGIQGPTG LPGIPGEIGR
QGPSGEPGIR GPAGPKGDSG KDGTHGTPGE QGIPGKPGLP GRQGDPGLNG QTGQKGDTGP
PGKSIEGPTG ATGSPGVQGP AGPPGPPGRT IIEADGGSGE VDGNGVKGPG QKGDKGDDGA
TGPAGPRGID GVPGIPGEPG PAGLPGLQGL RGEEGLVGLR GADGKDGKDG KAGPEGPSGP
PGVPGEKGER GLPGPVGVLP PGVTGGLGEK GEKGDSGEPG PMGPEGPQGP VGPRGFRGPK
GDIGMTGLPG YRGLRGRKGD RGRPGFNGLR GYKGDSGTPG PAGPPGLGFA GSGEILKGAK
GDKGDRGLPG IPGSPGIGAQ GPRGEPGEAG RNGLPGFQGP PGPAGPAGTG EAIRGPPGPP
GPPGPSGVGT NGGGGGGGAV TYRNRNELMS VARNLPVGTM CYLIEEEEVY LRVKKGFRLI
ELGEPVPLPP KTTPAPTKES APIIILPEGE MQSDQPRLYI FALNQPLSGR IGGIRGADAK
CHRQAKRAGK KGTYRAFLST KTQDLTSIVY YDIDKSVPIV NMKDQILFNS WKQLLNGHGG
YFNTQRHIYS FDGEDIMTSP RWPQKIVWHG STSNGNKVDD MTCNHWHTSS PRSMGYASSL
LDGKLVDMKE YSCSNRFIVL CVENTSRPMK
//
