ID A0A1A8A5V5_NOTFU Unreviewed; 1380 AA.
AC A0A1A8A5V5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSNFUP00015012594.1};
DE SubName: Full=Collagen, type XVIII, alpha 1 {ECO:0000313|EMBL:SBP49901.1};
GN Name=COL18A1 {ECO:0000313|EMBL:SBP49901.1};
OS Nothobranchius furzeri (Turquoise killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Nothobranchiidae;
OC Nothobranchius.
OX NCBI_TaxID=105023 {ECO:0000313|EMBL:SBP49901.1};
RN [1] {ECO:0000313|Ensembl:ENSNFUP00015012594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRZ {ECO:0000313|Ensembl:ENSNFUP00015012594.1};
RA Senf B., Petzold A., Downie B.R., Koch P., Platzer M.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SBP49901.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:SBP49901.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SBP49901.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:SBP49901.1};
RA Reichwald K., Felder M., Petzold A., Koch P., Groth M., Platzer M.;
RT "The genome of a short-lived fish provides insights into sex chromosome
RT evolution and the genetic control of aging.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSNFUP00015012594.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-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}.
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DR EMBL; HADY01011416; SBP49901.1; -; Transcribed_RNA.
DR Ensembl; ENSNFUT00015013225.1; ENSNFUP00015012594.1; ENSNFUG00015006171.1.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000694548; Chromosome sgr14.
DR Bgee; ENSNFUG00015006171; Expressed in caudal fin and 3 other cell types or tissues.
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; 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; 2.
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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:SBP49901.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW 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:UP000694548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044554907"
FT DOMAIN 117..306
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 312..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..411
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..591
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..742
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..804
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..910
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 141530 MW; 8E105D5F729535A4 CRC64;
MRIQFGVLFL LAQWVVCSDA WFWYWTGTTT LPPTVEHEGS GGLVGSGEPP FESGAVTGAE
IIDEQHGIQK VEQTLEETTK APELTTLTPA VEPTTQYASE TDTLEISSHT SNPEDNGVSL
LQLIGDPPPD GIPQVDGPDN NPGYVFGPDT SSGQMALAHF PSSFYRNFAL IFSVKPTSDQ
GGVIFSITDS SQEVIDVGVR LAAVQGGHQD VIFYYNYLGK KNSHEAARFP VPSMKDTWNW
FAIAVQDDKV MFYHSCEGEP QVMRMERSAD KLELESGAGV FVGGAGGSTH DKFEGVISEL
RVVGDPRAAE RLCEEEDDDS DMASGEGSGV EGSEVPNRYR EKHRYTTTTP SLPPIPQPPL
NRKGEEATVR ESGAVGAKGE KGERGDRGEK GDRGAIGPKG EAGSGFGSRG GIRGEKGEPG
ERGLKGNAGF GYPGKKGDPG PPGVPGPPGP PGPAAEYSVA SDGSVVSRVP GPRGPPGAPG
SQGPPGEDGE PGDPGEDGKT GPQGPPGFPG TPGDSGQKGE KGDRGEGQPG PRGLPGPPGA
PGPGYRSTFE DMEASGFSDL ETVRGPRGPP GPPGPPGPPG PSTSGSTSNS GAFGPPGKDG
APGLPGSPGL PGSDGPPGAP GPRGEKGDSG ELGLPGAIGQ KGAQGDLGLP GPPGEPGLAG
LPGPMGPVGP PGPAGPPGPS YRVGFDDMEG SSGLTGIRGP EGIQGSPGLP GHPGEPGLPG
ADGPKGDQGP TGKDGLPGLD GFPGPPGQKG DRGDKGETGD PGRDGTGLPG PPGPPGPPGQ
IIYQPSDRLD NFAGGAQGGL GLPGRAGLPG PVGPKGERGD PGPAGYGVKG EKGEPGLIIG
PDGAPLYLGG LTGQKGDRGP AGPVGPSGPY GPPGLKGEIG MPGRPGRPGV NGYKGEKGEP
GGGAGYGYPG VAGPPGPPGP PGPPGPAIPL DRYNAYDEAS RSYRVVKGDK GERGDRGPPG
TVSNFDIYTL KNQLKGDRGD TGVKGEKGEP GHGYYDPRIE GLQGPPGPPG NPGLPGPKGD
SIVGPSGPQG PPGPPGVGYD GRPGPPGPPG PPGPATSPSF TGTHRPHYPV SVPGPPGPPG
PPGNPGLSSG VTVLRSYDTM IATARQQPEG SLIYIIDKAD LYLRVREGLR QVMLGQYSPF
SRDLENEVVE VQPPPVIVYP HNSQNNGAGH YSDSGSVIRP IEPPQPRPHQ PVPGSTGLVE
TPESVLHLAA LNAPQTGDMR GIRGADFMCF QQARAVGLKG TFRAFLSSKL QDLYTIVRTL
DRKTFPIVNL KNQVLFTSWE SIFRENSSKM RENVPIYSFD GRDVLRDSAW PEKMVWHGSS
SEGKRNMDHY CETWRIDNHA LTGLASSLQS GYLLQQNRSS CSGSYIVLCI ENAFMSSSKK
//
