ID A0A9B0UAQ9_CHRAS Unreviewed; 1538 AA.
AC A0A9B0UAQ9;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_006876624.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_006876624.1};
OS Chrysochloris asiatica (Cape golden mole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Chrysochloridae; Chrysochlorinae; Chrysochloris.
OX NCBI_TaxID=185453 {ECO:0000313|Proteomes:UP000504623, ECO:0000313|RefSeq:XP_006876624.1};
RN [1] {ECO:0000313|RefSeq:XP_006876624.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_006876624.1};
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_006876624.1; XM_006876562.1.
DR GeneID; 102822431; -.
DR CTD; 80781; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000504623; 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 CDD; cd00110; LamG; 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; IPR001791; Laminin_G.
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; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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_006876624.1};
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:UP000504623};
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..1538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039609679"
FT DOMAIN 226..414
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 275..413
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 136..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..582
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..628
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..727
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..774
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 157502 MW; AD649DB2AC8CF1F7 CRC64;
MASDPSRHCS FLLLTCCLAT AHAELLGLEW LWGPNIVNPS KGLASQSRNN TPVQSLADPT
TNVMLQDAPT KQTTTPTAPE PPLERLEAAQ DGATTAPAAL GSIPDKREEN IAGVGAKILN
VAEGIRSFVQ LWDDTTSTKS PTGASTLAPV APTDPLTPSE SSDIPAGSGT APWASNTAPK
SQDTLRTHPS TLLAPTQMFP SLGRPRALLR EPLMPPPSPE NVGTEEVGLL QLLGEPPPPQ
VTQIEDPNFG PAYVFGPDAN SGQVARYHVP SPFFRDFSLL FHVKPTTESA GVLFAITDAA
QAEIRVGVKL SNVQDGHVQI QLLYTEPGTG HTRTAASFPL PSFTHRWIRF ALSVDGDTVV
LYVDCEEIQR LPFQRSPGGL ELEPGAGIFV GQAGGADPDK FQGLIAELKV RGDAQVSPLY
CLEEDGDDSD GASGDFGSGL EDNQEHPTEE MASPLKPKLP EAPPVTSPPL AGGSNTEDSR
TEEIEEETTM ATLGGKTVFS VWCVVYVTQT LPVVEHERSG STSPADSNVA ATLEGMKEGG
LKPSSTGLKG QKGEPGAQGL PGPAGPQGPA GPAVQSPDGP AAQPFPGPQG PPGPPGKDGT
PGKDGEPGDP GEDGKQGDPG PQGFPGTPGE IGLKGEKGDA GIGPRGPPGP QGPPGPPGPA
FRHDKLTFID MEGSGFGGDL ETLRGPRGFP GPPGPPGVPG LPGEPGRFGV NSSDVPGPAG
LPGVPGREGP PGRPGPQGHP GPPGKEGQQG ENGQKGSSGE VGAPGPKGGQ GDPGPVGAPG
KNGLVGAPGP AGPQGPPGPP GPPGPPGPGL AAGFDDMEGS GGPFWSTTGS SGPQVPTGLP
GFKGDPGMAG PPGTKGEVGE DGAPGFPGLP GKEGEQGPKG DKGSQGAKGD PGKDGVGQPG
LPGPPGPPGP VVYVSEDQDV ISSMSGNEGR LGHAGFPGPA GPKGDLGSRG EPGYPGQKGE
KGEPGTIFGH DGTILTSSQK GAKGEPGFRG PPGPYGRPGY KGEIGFPGRP GRPGMNGLKG
EKGEPGNDGA AFNMRCPPGP PGPPGLPGPP GMPVYDNNAF ANSGRPGPPG LPGYQGPSGP
KGDKGEVGPP GAPGQFPLDI LQLEADMKGE KGDRGHTGQK GERGEPGGGG FFGSSVPGPP
GPPGPPGYPG IPGPKGESVQ GQPGPPGPQG PPGIGYEGRQ GPAGPPGPPG PPGLPSFPGP
HRQTISVPGP PGPPGPPGPP GTTGASLGVR IWATYQTMLN KVHEVPEGWL IFVAEREELY
VRVRNGFRKV LLEARTPLPR GTDNEVAALK PPVVHEDRPY SSWQDHPQTT TRPWRSHSVL
ANPPRLPDPQ PYPGVPHHSS YMQLQPARPT FTPAHGHAHQ DFQPVLHLVA LNGPLTGGLR
GIRGADFQCF QQARAVGLSG TYRAFLSSRL QDLHSIVRRA DRGSVPIVNL KDEVLFPNWE
ALFSGSEGQL RPGAHIFSFD GRDVLRHPAW PQKSVWHGSD PSGRRLTESY CETWRTEGTS
VTGQASSLLA GRLLGQKAES CHNTFIVLCI ENSFMTSS
//
