ID A0A1S3JCH7_LINAN Unreviewed; 1362 AA.
AC A0A1S3JCH7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE SubName: Full=Collagen alpha-1(I) chain isoform X2 {ECO:0000313|RefSeq:XP_013407891.1};
GN Name=LOC106171914 {ECO:0000313|RefSeq:XP_013407891.1};
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_013407891.1};
RN [1] {ECO:0000313|RefSeq:XP_013407891.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013407891.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_013407891.1; XM_013552437.1.
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; 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: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 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 ECO:0000313|RefSeq:XP_013407891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..198
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 236..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..483
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..602
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..785
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1362 AA; 138309 MW; F0EC74D73D146FDB CRC64;
MGEPRESDLL QAIDVRPLTP HVTFISGFDG YPAFQIKHNA DIQKPVLSYL PKVLFAEFSI
LVTVEQFSAE GGFLFAVVNP MSNVLQFGLN ITEVVDGHQN IVLIYTELEK HKELEPTATA
IATFKVPQFV KQWSRFAILV YQESITLYLD CEEYETVTFE DRKPLMLIPG STLYIGQGGA
FGGHFQGAVQ ELKIHPDHRE AEDQCQENFI GSGSNPSDSG EDFTIASHLF SDFNGVTQPS
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 PGMPGLDGID GRPGVPGPPG PPGPSVSILS AAGEVNRIDP
DVIPIGREDL VPIKGEKGDP GRPGIPGFCH ASECQGLPGE PGRPGEPGPM GEIGMPGFPG
LRGAPGVGVP GPKGDQGAPG MKGEPGLPGR VEYVGNNGAD GSPVTVVGPP GPKGDTGDMG
PNGLPGFPGK PGREGPAGPI GPPGLPGSPG LSGQDGYPGK TGKQGPKGEK GDRGLRGPPG
VVTTVDGETL TGGVPGPEGP PGERGPPGPP GERVIGPPGL PGPPGVGIVG PPGPPGVGLP
GPPGPPGDPG NGILLGEAGK PQEATTGLYP LKAVTVEDKS ELHQLSNGVP VGSLVYVMVE
EKLYLRVGQG WQAVNLGYLE EIPEPTPPPT TTSAPLIPPP TGTEVVLGPR LHLIAANKPL
SGAMHGISGA DYQCYRQAKD AGMEGTFRAF LSSRVQNLDS VVFVKDRSVP IVNSKDQLLF
KSWDDIFKGV SFNNRIPILS FDGKDVMYDP KWPQKYIWHG ADSTGQRMMD AYCDAWDTSK
TEMTGMASSL RSNHLLDQEK YACSNSFVVL CVEITHRRNV RK
//
