ID A0A674NCI8_TAKRU Unreviewed; 1317 AA.
AC A0A674NCI8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSTRUP00000071465.1};
GN Name=col18a1a {ECO:0000313|Ensembl:ENSTRUP00000071465.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000071465.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000071465.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000071465.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSTRUP00000071465.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011610514.2; XM_011612212.2.
DR Ensembl; ENSTRUT00000073743.1; ENSTRUP00000071465.1; ENSTRUG00000032345.1.
DR GeneID; 101077615; -.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A674NCI8; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000005226; Chromosome 1.
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 GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
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:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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:UP000005226};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1317
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025552343"
FT DOMAIN 31..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..314
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..504
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..706
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..931
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 135040 MW; 3021C9D5F8CB6EC0 CRC64;
MKMRCARLQR LLCCVLVVIG LAASQWPEDN GVSLLQLIGD PPPPEITQVD GPENSPAYVF
GPDANTGQLA RAHLPSPFYR DFALIFHLKS SSNKGGVVFS ITDASQQIMY VGVKLSDVQG
RNQNIILFYT EPGSEESYEA ASFPVPSTVD TWTRFAIAVR DDKVMFYFNC EVDPLVMPIE
RSPDEMELEA GAGVFIGQAG GADPGKFLGV ISELRVVGDP RVAERYCEED GDDSDMASGE
GSGYEESRPP KPEEKHRWTT TPPPSRPIQQ PPLSTKEQVL RETGALGAKG EKGDRGERGE
KGGRGPSGPK GDSGFGSSSR GGARGEKGEA GAKGEKGSAG FGNQGTKGEP GSPGPPGPPG
PVGDSVSCKD GSAGNTCLQG PPGADGEPGV PGEDGKPGPQ GASGFPGTPG DQGPKGEKGD
TGEGPPGPRG PPGPPGPPGT GLRSTFVDME GSGYPDLESV RGPPGPPGIP GPPGPPGTPG
ASTAATGLGS GAAGPPGKDG APGQPGSPGL PGTDGSPGAT GPKGEKGNTG ELGLPGAVGQ
KGDQGSPGLP GSPGEAGLAG LPGPRGPMGL PGPPGPGYRV GFDDMEGSGG GFINRQPGVR
GPEGKQGPPG FPGLPGKPGF PGLPGPKGND GPEGKDGRPG LDGFPGPQGP KGDRGDKGDR
GEAGQDGTGL PGPPGPPGLP GEIIYRSSGN TDGAVGSVGP QGIPGQPGFP GPAGPKGDRG
EPGFPGFGEK GEKGEPGLAI GPDGYRLSLE GLTGLKGERG IPGPVGPPGP YGPPGLKGEI
GMPGRSGRPG INGYKGEKGE PGTGSGFAYP GPPGPPGPPG PPGPTINQDR FNRYDDTHRN
YPAVKGEKGE HGEQGLPGIP GTASNFDIYA YKNELKGERG DQGLKGEKGE SGGYYDPRFG
GVQGPPGTPG LPGPKGDSIT GPPGPQGPPG QPGIGYDGPA GSPGPPGPPG APGTSTYNYP
VSLPGPPGPP GPPGIPGHSS GVTVLRSYDT MIATARRQPE GNLIYIIDKA DLYLRVRNGL
RQVMLGNYSP FFRELENEVA EAQPPPVILY PHSQDQSHNN GAGHYSQGGP AIQPIDPPPQ
PPVNNNNYPP HYEPRVPETR HTGHTEGRSG TQTETQHPVT PQRPPNPPVL QPLGNVETSA
SALHLIALNA PHTGNMRGIR GADFLCFQQA RAIGLKGTFR AFLSSKLQDL YTIVRRSDRD
NFPIVNLKDQ VLFRSWESMF GDEASKITEN VPIYSFDGRD ILRDSAWPEK MVWHGSSNKG
HRQTDQYCET WRAGDRAVTG LASSLKSGYL LQQSASSCSG SYVVLCIENA FTSHSKK
//
