ID A0A1A8AKN6_NOTFU Unreviewed; 1533 AA.
AC A0A1A8AKN6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSNFUP00015001006.1};
DE SubName: Full=Collagen, type XVIII, alpha 1 {ECO:0000313|EMBL:SBP55742.1};
GN Name=COL18A1 {ECO:0000313|EMBL:SBP55742.1};
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:SBP55742.1};
RN [1] {ECO:0000313|Ensembl:ENSNFUP00015001006.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRZ {ECO:0000313|Ensembl:ENSNFUP00015001006.1};
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:SBP55742.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:SBP55742.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SBP55742.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:SBP55742.1};
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:ENSNFUP00015001006.1}
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; HADY01017257; SBP55742.1; -; Transcribed_RNA.
DR Ensembl; ENSNFUT00015001101.1; ENSNFUP00015001006.1; ENSNFUG00015000608.1.
DR GeneTree; ENSGT00940000165423; -.
DR OMA; WWKVSAS; -.
DR Proteomes; UP000694548; Chromosome sgr04.
DR Bgee; ENSNFUG00015000608; Expressed in caudal fin and 1 other cell type or tissue.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 2.
DR Gene3D; 2.60.120.200; -; 2.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:SBP55742.1};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1533
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044554974"
FT DOMAIN 34..224
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 281..466
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 239..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..538
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..640
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 158791 MW; E98E014504A2DCEF CRC64;
MHRRDRWSIL IWKTCSFFLL VVASIQSQQT KENGVDLHQL IGDPPPENIK KVFGLEYGHV
SYKFTSAAAL GQPALAHVPN PFYRDFSLMF YIKPTTPNAS VLFAITSSAQ NLMYIGVKLS
AVESGRQKVK FFYTEPGSES SYEAASFDVQ SMLNRWTVFS LSVADDQLTF YQGCYKKPQV
VKFERSPDPM EIDLASRIFV GHGGTADPDK FEGLIAKLKL VGDPRAVERF CEIEDDINEA
SGVSGEGSGE TNQHEDNTVR ATPQPSLVPK PIVIPSTDKS KVTLKQLVGD PLPAGITLEG
TSFYKFSSSG NVNQLALNHV PNPFYRIFSI VFRFQTSSAN AAVLFSITDS SQKLMLVGVK
LGPIKSNRQK LQFFYTEPGS EASTEAASFD IPARQSMFYT LGVTVFDDQV TLHMDCEKEP
QVVKFQRSPD PMVLDPGARL FLGQAGKADP NKFEGKFSEF TLEEGTQAFE SFCDYNDYSN
KELETVKVPV NDAGMTGSRG DKGDKGDKGE RGPKGDQGPA GPKGDSGSSS VSSSSSQSKE
QGLKGEKGAK GDSGFGYAGS KGERGPQGPP GPPGPPGPAA EVVKLAEGSV VHKVSGPPGP
PGSPGPAGAP GPPGDDGEPG DPGEDGKSGP AGPQGAPGLP GTSGTKGQKG ERGEGPPGPR
GPPGPPGPGT ADRSTFVDME GSGFPDLDKI RGPRGPPGPP GPPGIPGTSV ALGPDGPVAF
GPPGPPGRDG APGLPGRPGP PGPPGPPGPG GEKGDGGDLG LPGPAGEKQA EVDSNPFDYL
FSFFAPSSTG AQGDPGRTGT PGQTGLAGLP GPMGPVGPPG PPGPPGPPYI IRDGSKLGNE
VLNGLPGLRG PPGPQGPAGV PGLPGNPGFP GDHGIKGAEG PRGPSGIPGV DGYPGPPGVK
GDRGEKGETG LPGRDGGPPG PPGPPGPPGE VINSPTRDLE EVYWNEVGKG GSGRSGFPGS
VGQKGDKGDV GPPGYAPKGQ KGEPGIIFGP DGKPLYLGGL AGQPGEKGVP GPVGPPGPYG
PPGLKGEIGL PGRPGRPGFN GAKGEKGDSG SGSGYGYPGP PGPPGPPGPP GPPLSVDRIG
GYDGYPRNYA EKGEKGDQGP PGMLEISGLG ANFDLYTLKN ELKGETGLKG EKGEPGGYYD
PRYGGSAGGS PGVPGPPGPR GESIVGPPGP QGPPGSPGRG YDGRPGPPGP PGPPGPSLSG
PYRGTQTISI PGPPGPPGAP GLPGHSSGVM VLRTYESMAA TARRQPEGSL VYVIDQTDLY
LRVRDGVRQV QLGNYIPFPN APGDELGAVE PPPIVPYSPE YNRQPAQPDS QYPLQTDPRY
PSYADRFNRP DGRYIDPRQP VTPPRRPPPP QAALHSHTSG PALHLIALNS PHSGAMRGNS
GADFKCFSQA QAIGLKGTFR AFLSSKLQDI HSIVRRDDRE NVPIVNLKDE VLFDNWNAIF
SDGRMKDNVS IYSFNGKDVV RDDTWPEKMV WHGSTNGGQR HLDSFCESWR VSDRAVTGMA
TSLKSGSLTQ QTSSSCSSSY VVLCVENSYI GHA
//
