ID A0A6J3RBJ5_TURTR Unreviewed; 1409 AA.
AC A0A6J3RBJ5;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_033712136.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_033712136.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033712136.1};
RN [1] {ECO:0000313|RefSeq:XP_033712136.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033712136.1};
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}.
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DR RefSeq; XP_033712136.1; XM_033856245.1.
DR CTD; 80781; -.
DR Proteomes; UP000245320; Chromosome 4.
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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
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 ECO:0000313|RefSeq:XP_033712136.1};
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:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 119..308
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..449
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..594
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..642
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..719
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
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 801..825
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 143903 MW; E37FA1E456AFAD19 CRC64;
MGRHDAATAP TRLGRGRPAP LSSIRRPRRG TSLFKSPTFL LPHRTRGLRT NPLVTVTFPK
RRRAGHTACP WTLPRFAARD LRWPWLRPRR RRLLDLLAPV VLLLGVSAAS AEPESQVMEV
GLQLLLGEPL PRQVALVHDP DVGPAYEFGA DVGGDGWAAR SLLPSTFFQH FSLLVHVRPA
SARAGVLFAV TDAARAVVLV GVKLAAARGA WQQVQLLYTE PGAARTHTAA SFTLPALDGR
WTRLAIAVDG AHAALFVDCK EVQRQPLARS PRGLQLEPDA RLFVAQAGRA DPDKFQGLIS
DLRLREDPQV SPLHCLDEDE KDDDDRASGD LGSGLAETWE RIGEELGAPL GPGLPEAPPV
TSPPLAGVGS QEDFRTEEIE EETTVSSLGA QTLPSLSTVA TWDGGEWSPG GGLKEQGLKG
QKGEPGAQGP PGPVGPQGPA GPAVQSPDAQ PVPGPQGPPG PPGKDGAPGR DGEPGDPGED
GKPGDTGPQG FPGTPGDMGP KGEKGDPGVG PRGPPGPQGP PGPPGPSFRP DRLTFIDMEG
SGFGGDLESL RGPRGFPGPP GPPGVPGLPG EPGRFGMNSS DVPGPAGLPG VPGRDGPPGL
PGTPGPPGPP GKDGQPGQSG QKGSLGEAGA PGPKGSKGDP GPIGTPGEHG LAGRPGPAGP
PGPPGPPGPP GPGLAAGFDD MEGSGGPFWS TARGANGPQG PPGPPGVQGD PGVTGPPGTK
GEAGADGAPG FPGLPGREGA AGLQGPKGEK GPQGEKGDPG KDGVGQPGLP GPPGPPGPVV
YVSEQDRALA SVPGPEGRVG LAGLPGPAGP KGDLGSRGQQ GLPGPKGEKG EPGMVFSPDG
RALTSAQKGA KGEPGFRGPP GPYGRPGHKG EIGFPGRPGR PGMNGLKGEK GEPGDASVGF
SARGPPGPPG PPGPPGPPGT PVYDSNAFVE SGRPGPPGLP GHQGPSGPKG DKGEVGPPGP
PGQFPLDLLH LGAEMKGEKG DQGAAGQKGE RGEPGGGGFF GSSVPGPPGP PGYPGIPGPK
GESIQGQPGP PGPQGPPGIG YEGRQGPPGP PGPPGPPGPP SFPGPYRQTI SVPGPPGPPG
PPGPPGSMGT SSGVRVWATY QTLLDQVHDV PEGWLIYVAD REELYVRVRN GFRKVLLEAR
TPLPRGTDNE VAALQPPVVQ LHEGNPYPRR EPPHPTARSW PRQDRRADDI LASAPRLTHA
QPYPGAPHPG AYAHHRPATP TASPAHTHHD FQPVLHLVAL NSPQSGGLRG IRGADFQCFQ
QARAAGLAGT FRAFLSSRLQ DLYSIVRRAD RATLPIVNLR DEVLSPSWEA LFSGSEGQLK
PGARIFSFDG RDVLQHPAWP QKSLWHGSDP SGRRLTESYC ETWRTEARAA TGQASSLLAG
RLLEQRAASC HSAFIVLCIE NSFTASSSK
//
