ID A0A6J3RC28_TURTR Unreviewed; 1400 AA.
AC A0A6J3RC28;
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 X3 {ECO:0000313|RefSeq:XP_033712137.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_033712137.1};
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_033712137.1};
RN [1] {ECO:0000313|RefSeq:XP_033712137.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033712137.1};
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_033712137.1; XM_033856246.1.
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:0032836; P:glomerular basement membrane development; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 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_033712137.1};
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..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1175
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 791..815
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 143053 MW; E7A0A05670ADB6B9 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
YVSEQDGRVG 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
SSGQVRVWAT YQTLLDQVHD VPEGWLIYVA DREELYVRVR NGFRKVLLEA RTPLPRGTDN
EVAALQPPVV QLHEGNPYPR REPPHPTARS WPRQDRRADD ILASAPRLTH AQPYPGAPHP
GAYAHHRPAT PTASPAHTHH DFQPVLHLVA LNSPQSGGLR GIRGADFQCF QQARAAGLAG
TFRAFLSSRL QDLYSIVRRA DRATLPIVNL RDEVLSPSWE ALFSGSEGQL KPGARIFSFD
GRDVLQHPAW PQKSLWHGSD PSGRRLTESY CETWRTEARA ATGQASSLLA GRLLEQRAAS
CHSAFIVLCI ENSFTASSSK
//
