ID A0A6P5JD14_PHACI Unreviewed; 1512 AA.
AC A0A6P5JD14;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-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_020829016.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_020829016.1};
OS Phascolarctos cinereus (Koala).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Phascolarctidae; Phascolarctos.
OX NCBI_TaxID=38626 {ECO:0000313|Proteomes:UP000515140, ECO:0000313|RefSeq:XP_020829016.1};
RN [1] {ECO:0000313|RefSeq:XP_020829016.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_020829016.1};
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_020829016.1; XM_020973357.1.
DR GeneID; 110198839; -.
DR CTD; 80781; -.
DR Proteomes; UP000515140; Unplaced.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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_020829016.1};
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 Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000515140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..387
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 393..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..414
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..585
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..687
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..961
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 155002 MW; 7C98AB49AE9E509C CRC64;
MTTAGNWGCW WPISLGTVMV LFLMPLLWWA LLASMPLGLG GLICYLLLGI SLALATRTGC
PPPCQDWLRP RGTACRCQPI YPSAATPAPS ASGCPTTPTM TVPSRCGRPC KSGRGCCAHG
ATASLKPSSA CCSCPSVAPP IPCCRRHHAG SSVRAFETCA GASCTRAGCP CPAPHSQPRG
DAQQACVFID VTAENFSAEV SLPQLIGQPP PKHISQIDDP DIGLAYVFGP NANSGQVARY
HVPNPFYRDF SLLFHIKPTS ERAGVLLALT DAAQAVIAMG VKISEPYSGK QDVLFFYTEP
GVGETRTAAS FSLPSFVNQW TRFAISVDGD EVALYVNCKE IQRLPLDRSL QELELEPGAG
LFVAQAGGAD PDKFQGVISE LKMRGDPRVT LLQCLDDDDD DSDGASGDFG SGADEQGGPS
GSDMGPPLSP SLPMPPPVTL LPLDTTTMSL QPGLVKVEGA HVSSSGARLD SRGEEGARGP
TRPEGTLDQA RRITEEGTRY MSPGLKGQKG EPGVQGPPGP VGPQGPAGPA IPSPDGSTVQ
QVPGPQGPPG PTGPPGKNGE PGDPGEDGKP GEMGPQGFPG TPGDVGPKGD KGDPGTGPRG
PPGPPGPPGP PGPAFRPDKL TFIDMEGSGF GGDPESLRGP RGFPGPPGPP GVPGLPGEPG
RFGMNSTDGP APPGLPGVPG RDGSPGLRGP PGPPGLPGKD GQPGEQGQKG DRGDMGSPGP
QGSKGDIGPV GAPGETGLAG LPGPMGPRGL PGPPGPPGPP GAGWAAGFDD MEGSGLPFWT
AVPGTRGAEG PQGLPGFPGL KGDRGSVGQP GEKGDPGFPG PPGSEGMPGP QGPKGDPGSQ
GQKGEPGKDG VGQPGPPGPP GPPGEMTYVS EEGKTFASVS GREGRPGYAG FPGPAGPKGD
TGAHGPQGSP GAKGEKGEPG SVLTLSEKGA KGDQGYRGPP GPYGRPGHKG EIGIPGRPGR
PGMNGLKGEK GEPADANRAV GPRGPPGLPG PPGPPGAPGL LGTSFYDNNG FLEPGRPGPP
GLPGYQGSPG PKGDKGEAGP AGPPGILPYD FSTLVEHMKG EKGEEGVKGE KGEPGSGGFF
SSGVPGLPGP PGPPGYPGVP GPKGESIRGQ PGPPGPQGPP GIGYEGRQGP PGPPGPPGPP
SFPGPHRQTI SVPGPPGPPG PPGPPGTSGT SSGQLRIWTS YQAMLNKAHE VPEGWLVYVA
EREELYVRVR RGFKKVLLEA QTVLSRGADN EVAVLQPPIV EYSPGNSAPS GSHIQDGNLP
YPHRGYPHST AKPWRADDIQ ANHPRFSEHG GHHPPYHGVQ QHPHDRIPSY HGSYTNVRPA
QPTASPLHVH HDFQPALHLV ALNGPQTGSM RGIRGADFQC FQQAREVGLM GTFRAFLSSR
LQDLYSIVRR ADRGSVPIFN LQDEMLFDSW EALFSGSEGQ LKPGSRILSF DGKDVLRHSA
WPQKSVWHGS DAKGRRLTES YCETWRTDEG AATGQASSLF SGKLLEQKAV SCRNSFIVLC
IENSFMTSSS KK
//
