ID A0A2I4BSF8_AUSLI Unreviewed; 1647 AA.
AC A0A2I4BSF8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_013870648.1};
GN Name=LOC106522253 {ECO:0000313|RefSeq:XP_013870648.1};
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_013870648.1};
RN [1] {ECO:0000313|RefSeq:XP_013870648.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_013870648.1; XM_014015194.1.
DR GeneID; 106522253; -.
DR KEGG; alim:106522253; -.
DR InParanoid; A0A2I4BSF8; -.
DR OrthoDB; 5983381at2759; -.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_013870648.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000192220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 218..344
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 50..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..96
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..707
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1065
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1171
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 277..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1647 AA; 173282 MW; 79299E69388586E1 CRC64;
MGSDKSESES DLGSGLLFSS ESDFIAGNEK SLGSGKEAGT SIHYGWLDRG ASAGSMKNEQ
KRKFTEKTSP NRVDQDQNLD SAAKTPNNQN NINNNTRRND FNLTSYKTPE DFIPLNLNGS
XAQAAEVSQS NQQLKDSQMP NEDILPNMLK TEQVPVLNQT LSITETQTHN LFIAQSKTHN
NRPESNSAPT ETQLQISSET LREKALTGQT AEVLAENHTE VKSKPVIESS QCLLIDTALP
FCFSMEGFAV PNYLNQSSVE EVRTLLNEWV WLLQSRCHPS LERFFCLLLV PKCGSGAAPP
VLPCQSFCEV LRDSCWTLLD EGHLPVECHS LPDEEDEGYQ CLSXSNRKED NSVSLLELIG
DPPPDEIPKV EGPNNNPGYL FGPDTNTGQL AHAHFPGSFY RNFALIFNMK PTSDNGGVLF
SITDPSQEII HVGVKLSAVR GAKQDIIFYY TEPGSEQSKE AARFQVPSMT NMWNWFAISV
KDDKVMLYLN CDGETEVKSI ERSTDNLDLE LAAGVFVGRT GGSKPDKFEG VISELRVVGD
ARPVERLCEE DEDDSDVASG EGSGNEETRL SNHYRDKPRY TTSSPSFPPI PQPPLRIKGE
DASIRETAGD SEHFLVSAES RRLGAAGAVA TKGAKGDKGD KGEKGDRGPI GPKGESGSAS
RSQGANRGDK GEPGEKGSKG NAGFGYQGKK GEPGLPGPPG PQGPPGPATE YSVGSDGSVA
SKVPGPQGPP GPPGPQGPPG EDGEPGDPGE DGKTGPQGPP GFPGTPGDPG SKGEKGDRGE
GQPGPRGPPG LPGPPGPGFR STFEDMEASG FSDLEKVQGP PGPPGPPGPP GPPGSPVSGP
ALSSGAFGPP GKDGAPGQPG LPGLPGADGL PGAPGPRGEK GDSGDLGLPG AIGEKGAPGQ
PGLPGPPGET GLAGLPGPMG PIGRPGPPGP PGPGYRVGFV TWRGPVEVPP VDLQASEDQK
EFRVRQVYQD TQVSLVCLVY KVQRGIRVRL EKMDYXAWTA SLDPRVKRVT EGTEERGVSR
VEMELDHQVY QVHLDHQDKS STSHLTTFDN FAGSVGAQGG PGSPGRAGFP GPVGPKGDRG
DPGPPGYGLK GEKGEAGFII GPDGNPLYLG GLTGPKGERG PPGPVGPPGL QGPPGNKGEF
GMPGRPGRPG VNGYKGEKGE PGGGSGYGYP GFPGPPGPPG PPGPPGPALP LDRFNRYDET
PRTSQAIKGE KGERGERGIP GIPGTASNFD IYAFKNELKG ERGDSGAKGE KGEPGAGYYD
PHFGGLQGPP GPPGSPGLPG PKGDSIMGPP GPQGPSGPPG VGYDGRPGPQ GPPGPPGPPG
SSTFSGSYQP NYPVSVPGPP GPPGPPGSPG HSSGVTVLRS YDTMIATARQ QQEGSLIYIL
DNADLYLRVR DGLRQVMLGE YSSLFGGLGN EVAEVQPPPV ILYPHSPDRP HNNGAGHYSE
SGSVIRPIEP PQQHPNPPVP GPAVRVETSE SGLHLVALNT PQTGNMRGIR GADFMCFQQA
RAVGLKGTFR AFLSSKLQDL YTIVRRQDRS SFPIVNLKNQ KLFDSWESIF SDDSSRMREN
VPIYSFDGRD ILRDSAWPEK MIWHGSSSKG HRQMDHYCET WRAGDRAVTG LASSLQSGHL
LQQTPSSCSG SYIVLCIENA FMSPSKK
//
