ID A0A6P5J3W4_PHACI Unreviewed; 1466 AA.
AC A0A6P5J3W4;
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 X4 {ECO:0000313|RefSeq:XP_020829017.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_020829017.1};
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_020829017.1};
RN [1] {ECO:0000313|RefSeq:XP_020829017.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_020829017.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_020829017.1; XM_020973358.1.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:TreeGrafter.
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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 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_020829017.1};
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:UP000515140};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027791693"
FT DOMAIN 153..341
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 77..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..368
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..641
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..915
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1054
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 150547 MW; DE5858B6D0BA4B3B CRC64;
MAPLQSSLAL LLLLVAHCPL SRAQFFNWWT LKETEATVGP LLPTSGPQVK STPFAGPTVP
SATLAAQTGI LRPIPEEQPA SGLWTQPDPE ASEATGAVTP LRAPPARTDL KEENIAGVGA
KILNVAQGIR SLVQFWDEKS NGESSSKENF SAEVSLPQLI GQPPPKHISQ IDDPDIGLAY
VFGPNANSGQ VARYHVPNPF YRDFSLLFHI KPTSERAGVL LALTDAAQAV IAMGVKISEP
YSGKQDVLFF YTEPGVGETR TAASFSLPSF VNQWTRFAIS VDGDEVALYV NCKEIQRLPL
DRSLQELELE PGAGLFVAQA GGADPDKFQG VISELKMRGD PRVTLLQCLD DDDDDSDGAS
GDFGSGADEQ GGPSGSDMGP PLSPSLPMPP PVTLLPLDTT TMSLQPGLVK VEGAHVSSSG
ARLDSRGEEG ARGPTRPEGT LDQARRITEE GTRYMSPGLK GQKGEPGVQG PPGPVGPQGP
AGPAIPSPDG STVQQVPGPQ GPPGPTGPPG KNGEPGDPGE DGKPGEMGPQ GFPGTPGDVG
PKGDKGDPGT GPRGPPGPPG PPGPPGPAFR PDKLTFIDME GSGFGGDPES LRGPRGFPGP
PGPPGVPGLP GEPGRFGMNS TDGPAPPGLP GVPGRDGSPG LRGPPGPPGL PGKDGQPGEQ
GQKGDRGDMG SPGPQGSKGD IGPVGAPGET GLAGLPGPMG PRGLPGPPGP PGPPGAGWAA
GFDDMEGSGL PFWTAVPGTR GAEGPQGLPG FPGLKGDRGS VGQPGEKGDP GFPGPPGSEG
MPGPQGPKGD PGSQGQKGEP GKDGVGQPGP PGPPGPPGEM TYVSEEGKTF ASVSGREGRP
GYAGFPGPAG PKGDTGAHGP QGSPGAKGEK GEPGSVLTLS EKGAKGDQGY RGPPGPYGRP
GHKGEIGIPG RPGRPGMNGL KGEKGEPADA NRAVGPRGPP GLPGPPGPPG APGLLGTSFY
DNNGFLEPGR PGPPGLPGYQ GSPGPKGDKG EAGPAGPPGI LPYDFSTLVE HMKGEKGEEG
VKGEKGEPGS GGFFSSGVPG LPGPPGPPGY PGVPGPKGES IRGQPGPPGP QGPPGIGYEG
RQGPPGPPGP PGPPSFPGPH RQTISVPGPP GPPGPPGPPG TSGTSSGQLR IWTSYQAMLN
KAHEVPEGWL VYVAEREELY VRVRRGFKKV LLEAQTVLSR GADNEVAVLQ PPIVEYSPGN
SAPSGSHIQD GNLPYPHRGY PHSTAKPWRA DDIQANHPRF SEHGGHHPPY HGVQQHPHDR
IPSYHGSYTN VRPAQPTASP LHVHHDFQPA LHLVALNGPQ TGSMRGIRGA DFQCFQQARE
VGLMGTFRAF LSSRLQDLYS IVRRADRGSV PIFNLQDEML FDSWEALFSG SEGQLKPGSR
ILSFDGKDVL RHSAWPQKSV WHGSDAKGRR LTESYCETWR TDEGAATGQA SSLFSGKLLE
QKAVSCRNSF IVLCIENSFM TSSSKK
//
