ID A0A6P5J434_PHACI Unreviewed; 1536 AA.
AC A0A6P5J434;
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 X2 {ECO:0000313|RefSeq:XP_020829015.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_020829015.1};
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_020829015.1};
RN [1] {ECO:0000313|RefSeq:XP_020829015.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_020829015.1};
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_020829015.1; XM_020973356.1.
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: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; IPR010363; DUF959_COL18_N.
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; 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_020829015.1};
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..1536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028356903"
FT DOMAIN 224..412
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 78..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..439
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..610
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..712
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..986
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1536 AA; 157231 MW; D4858A97EB0DC51C CRC64;
MAPLQSSLAL LLLLVAHCPL SRAQFFNWWT LKETEATVGP LLPTSGPQVK STPFAGPTVP
SATLAAQTGI LRPIPEEQPA SGLWTQPDPE ASEATGAVTP LRAPPARTDL KEENIAGVGA
KILNVAQGIR SLVQFWDEKS NGESSSKGEA VAADPPATLP PLPSASGPGM ELRDAGKGST
GAPTPAGWTD AVHLTAATSP LGNRSPALPL GWPSAPPPEN FSAEVSLPQL IGQPPPKHIS
QIDDPDIGLA YVFGPNANSG QVARYHVPNP FYRDFSLLFH IKPTSERAGV LLALTDAAQA
VIAMGVKISE PYSGKQDVLF FYTEPGVGET RTAASFSLPS FVNQWTRFAI SVDGDEVALY
VNCKEIQRLP LDRSLQELEL EPGAGLFVAQ AGGADPDKFQ GVISELKMRG DPRVTLLQCL
DDDDDDSDGA SGDFGSGADE QGGPSGSDMG PPLSPSLPMP PPVTLLPLDT TTMSLQPGLV
KVEGAHVSSS GARLDSRGEE GARGPTRPEG TLDQARRITE EGTRYMSPGL KGQKGEPGVQ
GPPGPVGPQG PAGPAIPSPD GSTVQQVPGP QGPPGPTGPP GKNGEPGDPG EDGKPGEMGP
QGFPGTPGDV GPKGDKGDPG TGPRGPPGPP GPPGPPGPAF RPDKLTFIDM EGSGFGGDPE
SLRGPRGFPG PPGPPGVPGL PGEPGRFGMN STDGPAPPGL PGVPGRDGSP GLRGPPGPPG
LPGKDGQPGE QGQKGDRGDM GSPGPQGSKG DIGPVGAPGE TGLAGLPGPM GPRGLPGPPG
PPGPPGAGWA AGFDDMEGSG LPFWTAVPGT RGAEGPQGLP GFPGLKGDRG SVGQPGEKGD
PGFPGPPGSE GMPGPQGPKG DPGSQGQKGE PGKDGVGQPG PPGPPGPPGE MTYVSEEGKT
FASVSGREGR PGYAGFPGPA GPKGDTGAHG PQGSPGAKGE KGEPGSVLTL SEKGAKGDQG
YRGPPGPYGR PGHKGEIGIP GRPGRPGMNG LKGEKGEPAD ANRAVGPRGP PGLPGPPGPP
GAPGLLGTSF YDNNGFLEPG RPGPPGLPGY QGSPGPKGDK GEAGPAGPPG ILPYDFSTLV
EHMKGEKGEE GVKGEKGEPG SGGFFSSGVP GLPGPPGPPG YPGVPGPKGE SIRGQPGPPG
PQGPPGIGYE GRQGPPGPPG PPGPPSFPGP HRQTISVPGP PGPPGPPGPP GTSGTSSGLR
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
//
