ID A0A1S3JDC9_LINAN Unreviewed; 1147 AA.
AC A0A1S3JDC9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 40.
DE SubName: Full=Collagen alpha-1(I) chain isoform X5 {ECO:0000313|RefSeq:XP_013407894.1};
GN Name=LOC106171914 {ECO:0000313|RefSeq:XP_013407894.1};
OS Lingula anatina (Brachiopod) (Lingula unguis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013407894.1};
RN [1] {ECO:0000313|RefSeq:XP_013407894.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013407894.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_013407894.1; XM_013552440.1.
DR AlphaFoldDB; A0A1S3JDC9; -.
DR GeneID; 106171914; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000085678; Unplaced.
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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 6.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_013407894.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 905..943
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 976..1138
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 20..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..263
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..382
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..565
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..687
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 114723 MW; 370A71C97D7041B7 CRC64;
MKYQNFVFYS WVAAFVTQPS TGVTDSSGNS KGEVGNIGLL IPPPITPPPP EYPYYKGDKG
EKGDTGPAGP KGDRGLTGQQ GYSGLSGSKG EKGDRGSKGD QGPPGPPGPG VDSAVVPPPV
VVGPGGRVVN ASTSPLIIRG RGPKGQKGSQ GEAGFPGLDG LPGFPGQTGP KGTKGDVGAQ
GLPGIKGSKG EPGVFVGPLL NSGEGVTGPK GDKGDKGDRG EIGMIGLDGL PGAKGDKGDS
IVGPKGEPGR DGTTGPQGPP GNTVFIEGSG DNEGPTGPKG EPGLDGREGP VGPKGQKGER
GEVIQDNTVI VGPPGRDGVN GSRGPPGLPG LPGRPGEHGE AGPRGLKGDR GDIGPVGEQG
LPGPKGDRGE FGPQGLPGAR GLPGPPGPPG ITLESVGLTS SGDGDFGSGK PGPTGPRGFP
GNPGTPGLQG EPGLMGQKGE RGEKGEHGVK GERGFQGADG PQGFKGDMGD PGQPGVPGTP
GLEGEPGVKG EKGEKGEKGV GEPGPMGLMG PPGPPGLRGL PGLETESSGD IGLGEKGDPG
PPGLPGIIGP PGYPGLKGEP GLPGLDGRDG KDGKPGPPGS PGMPGLDGLD GRPGLPGPPG
PPGQVSQGLS HSNQWTNQID PGVINIPFGS LRKVESPEKG EKGDPGRPGI PGFCHASECQ
GLPGEPGRPG EPGPMGEIGM PGFPGLRGAP GVGVPGPKGD QGAPGMKGEP GLPGRVEYVG
NNGADGSPVT VVGPPGPKGD TGDMGPNGLP GFPGKPGREG PAGPIGPPGL PGSPGLSGQD
GYPGKTGKQG PKGEKGDRGL RGPPGVVTTV DGETLTGGVP GPEGPPGERG PPGPPGERVI
GPPGLPGPPG VGIVGPPGPP GVGLPGPPGP PGDPGNGILL GEAGKPQEAT TGLYPLKAVT
VEDKSELHQL SNGVPVGSLV YVMVEEKLYL RVGQGWQAVN LGYLEEIPEP TPPPTTTSAP
LIPPPTGTEV VLGPRLHLIA ANKPLSGAMH GISGADYQCY RQAKDAGMEG TFRAFLSSRV
QNLDSVVFVK DRSVPIVNSK DQLLFKSWDD IFKGVSFNNR IPILSFDGKD VMYDPKWPQK
YIWHGADSTG QRMMDAYCDA WDTSKTEMTG MASSLRSNHL LDQEKYACSN SFVVLCVEIT
HRRNVRK
//
