ID A0A2I4D062_AUSLI Unreviewed; 1248 AA.
AC A0A2I4D062;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_013885636.1};
GN Name=LOC106533750 {ECO:0000313|RefSeq:XP_013885636.1};
OS Austrofundulus limnaeus (Annual killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae;
OC Austrofundulus.
OX NCBI_TaxID=52670 {ECO:0000313|Proteomes:UP000192220, ECO:0000313|RefSeq:XP_013885636.1};
RN [1] {ECO:0000313|RefSeq:XP_013885636.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_013885636.1; XM_014030182.1.
DR GeneID; 106533750; -.
DR KEGG; alim:106533750; -.
DR InParanoid; A0A2I4D062; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000192220; 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 FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 3.
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_013885636.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1248
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014193909"
FT DOMAIN 37..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 226..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..406
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..511
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..666
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..793
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..943
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..988
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 128423 MW; 84B550215E6F1726 CRC64;
MTSCIPPWSI GFSLLLRLCC LHSSAYQLLE GLGSQSDLDL TELIGVPLPP SISFVTGFEG
YPAYSFGPYA NVGRLTKSFI PDPFYHDFAI TVTAKPTTRR GGVLFAITDA YQKIVQLGVA
LSEVEDGAQS IILYYTDPET RDGTQEAASF KMGDLTGRWA RFTLTVQGAE IRLYMDCEEY
HKVAFTRSAH PLTFDASSGI FVGNAGGTGL TRFVGSIQQL LLKSDATAPD DQCEEDDPYA
SGYGSGEEDY GDRNEIEEVK KIVEEREYTM PLPELDPTYS GPVRAPPTEV PLSDDEDMEE
SSGQDFETTI NKVRSFPTRA PAFEPDSVIG GQKGERGEPG PAGPPGAPGS PGKASDARGE
PGPKGPQGAQ GYQGVPGRPG TPGQPGSKGE LGSPGPTGFP GEQGEPGPKG EKGDPGVGRP
GPPGPPGPPG PPNKSSVALL EGSGFEDFDN DAEIIRGPPG PPGPPGLPGP PGTPSADVAL
GPPGAPGKDG KDGKKGEPGL PGVDGGDGDP GPAGEKGDKG EPGVSGQPGP KGDLGPPGFP
GLPGSPGPEG QPGPRGLPGP PGPPGPVGRG FDRTFEDLEG SGMLGDFESI PIPQGPPGIR
GPQGPKGKXG LDGIPGPPGQ KGEPGVRGPP GIPGFEGLKG AEGQKGDKGD PGQKGQAGRD
GLSLPGLPGP PGPPGPVTNL RDMLLNSTDG AFNFSGIFEA QGFAGPQGPK GDIGLPGLQG
PQGLKGEKGE PASVIAADGS LMFDMAGSTM PKGIKGDRGV TGPPGITGPI GPPGIKGEIG
IPGRPGXSGL IGPKGEKGDP QGRPGPPGPP GPPGRPGVFN CPKGKXIAKY SCMMHAIPGM
VKAQCKEITE PNSGGTIATG YCQQGPKGEK GDTGPPGLPA PPSTYLSKGT WGDKGSKGEK
GEKGDAGYPG QPGFPGRSGL VGPKGESVLG PPGQPGMPGP PGNPGYGRPG SVGPPGPPGP
PGTPGFLSGY GSALSIAGPP GPPGPPGSPG ASSNSATLKT FSTRESMMQQ TLRVEEGTLA
YVRATGSLFL KVSQGWKEIQ LGNLIYLSSN ILQQDEPQAA NQVRGQAVQR IRSIKQRLNL
VALNQPHSGN MLGLNRADRM CYEQAKAMGL APNYRAFIST NRQDLKNVVY PAFRENLPVT
NLRGDVLFLN WRSIFRGDSG TINTRIPIFS FDGRDVSADS FWPRKSIWHG SGNRGVRLLD
KHCETWQADD ISVMGQSSSL TSGLLLGQET RSCSNEYIVL CIETHKTY
//
