ID A0A6J3RDZ4_TURTR Unreviewed; 1391 AA.
AC A0A6J3RDZ4;
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 X4 {ECO:0000313|RefSeq:XP_033712138.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_033712138.1};
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_033712138.1};
RN [1] {ECO:0000313|RefSeq:XP_033712138.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033712138.1};
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_033712138.1; XM_033856247.1.
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; 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 ECO:0000313|RefSeq:XP_033712138.1};
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..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1166
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 886..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 142232 MW; AF0491058ED0C74C 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
YVSEQDGPAG PKGDLGSRGQ QGLPGPKGEK GEPGMVFSPD GRALTSAQKG AKGEPGFRGP
PGPYGRPGHK GEIGFPGRPG RPGMNGLKGE KGEPGDASVG FSARGPPGPP GPPGPPGPPG
TPVYDSNAFV ESGRPGPPGL PGHQGPSGPK GDKGEVGPPG PPGQFPLDLL HLGAEMKGEK
GDQGAAGQKG ERGEPGGGGF FGSSVPGPPG PPGYPGIPGP KGESIQGQPG PPGPQGPPGI
GYEGRQGPPG PPGPPGPPGP PSFPGPYRQT ISVPGPPGPP GPPGPPGSMG TSSGQVRVWA
TYQTLLDQVH DVPEGWLIYV ADREELYVRV RNGFRKVLLE ARTPLPRGTD NEVAALQPPV
VQLHEGNPYP RREPPHPTAR SWPRQDRRAD DILASAPRLT HAQPYPGAPH PGAYAHHRPA
TPTASPAHTH HDFQPVLHLV ALNSPQSGGL RGIRGADFQC FQQARAAGLA GTFRAFLSSR
LQDLYSIVRR ADRATLPIVN LRDEVLSPSW EALFSGSEGQ LKPGARIFSF DGRDVLQHPA
WPQKSLWHGS DPSGRRLTES YCETWRTEAR AATGQASSLL AGRLLEQRAA SCHSAFIVLC
IENSFTASSS K
//
