ID A0A7E6D2Z8_9CHIR Unreviewed; 1517 AA.
AC A0A7E6D2Z8;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X7 {ECO:0000313|RefSeq:XP_035873401.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_035873401.1};
OS Phyllostomus discolor (pale spear-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae;
OC Phyllostominae; Phyllostomus.
OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_035873401.1};
RN [1] {ECO:0000313|RefSeq:XP_035873401.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_035873401.1};
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_035873401.1; XM_036017508.1.
DR GeneID; 114489741; -.
DR CTD; 80781; -.
DR Proteomes; UP000504628; Chromosome 2.
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 Pfam; PF13385; Laminin_G_3; 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_035873401.1};
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:UP000504628};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028956262"
FT DOMAIN 233..421
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 44..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..736
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 154994 MW; F1C8DFED024A8896 CRC64;
MAPDPSGRLG WPLQLLLLFS CCFAATWADL LTWPWSSTQT NESTASLVSV PPGSPPVQPT
EGIITQVDPQ DGPTEQGMAS ASPEPPPERL EAAQGKASTS PPASVASRTS PDTKDTENIA
GVGARILNVA MGIRSFVRLW DDTTPAEDAS KMETLAPATP TDPLTLPGPS STPQENGTAR
WLTSGALHSP DTKKTEAGSL PAPTQPPPSP DGPWATLSVP SVPPKSSEKV GTEVGLLQLL
GEPLPPEITQ TDDPDVGPAY VFGSDANSGQ AAQYHFPSPF FRDFSLLFHV RPQTEGAGVL
FAITDTAQAV ISVGVKLSGV SDGHQHIQFL YTEPGAAQTH TAASFRLPAF VGQWTRFALS
VDGDTVTLFV DCEEVQSAPL VRSPRGLELE PGSGLFVAQG GDADPDKFQG MIAELRVRRD
PQVSPTHCLE DDDDDDDDGA SGDFGSGQEE TRGLLRKETG TPLEPSFPEA PPVTSPPLAG
GNVSEDSRTE EIEEQSTVSL LGAHTLPGSN TVTTWGRGVQ SPEDVLKEGL PGPVVQSPDA
RAIPGPQGPP GPPGPPGKDG APGRDGEPGD PGEDGKPGDI GPQGFPGTPG DVGPKGEKGD
PGVGPRGPPG PQGPPGPPGP SFRHDKLTFI DMEGSGFSGD LESLRGPRGL PGPPGPPGVP
GLPGEPGRFG VNSSVIPGPA GLPGVPGRDG NPGLPGPQGP PGVPGKDGRP GEAGQKGSLG
KVGTPGPKGS KGDPGPMGTP GENGLAGPPG PAGPQGPPGP PGPPGPPGPG LPAGFDDMEG
SGGLRIQDDT EGSGGPYWLA ARRADGLQGP PGRPGVKGDP GIPGLPGAKG EVGAGGPPGF
PGLPGREGMD GAQGPKGEKG TQGEKGDPGK DGVGQPGPPG PPGPPGPVVY VSEQDRAVAL
ARGAKGQPGY AGLPGPAGPK GDLGSRGQQG PPGPKGEKGE PGAVSGPDGR VLGLALKGAK
GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GMNGFKGEKG EPGDAIGIGT RCPPGPPGPP
GSPGPPGPPG LPRTPAYDSN AFMESGPAGP RGLPGHQGPS GPKGDKGEVG PPGPPGQFPF
DIFQLEEEVK GDKGDRGDSG QKGEKGEPGG GGFFGSSVPG PPGPPGYPGS PGPKGESIRG
QPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PGPPSFPGPY RQPISVPGPP GPPGPPGPPG
TVGTSSGVRI WPTYQTMLDK VPEVPEGWLM FVAEREELYV RVRNGFRKVL LEARTPLPRG
TDNEVAALRP PLVQLHEGNP HPRWELPPAT SRPWRADDIL ARPPRLLDPQ PYPGVPHHGS
YVHPWPARPT GVPAHTHQDF HPVLHLVALN GPQPGGLRGI RGADLQCFQQ ARAAGLAGTF
RAFLSSRLQD LYSIVRRADR ATVPIVNLWD EELFPSWEAL FSGSRGQLKP GARILSFDGR
DVLQHPAWPQ KSVWHGSDPS GRRLTESYCE TWRTEATTAT GQASSLLAGR LLEQKAASCH
NAFIVLCIEN SFMTSSN
//
