ID A0AAJ7WJH8_9ACAR Unreviewed; 1186 AA.
AC A0AAJ7WJH8;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_028969161.1};
GN Name=LOC100907162 {ECO:0000313|RefSeq:XP_028969161.1};
OS Galendromus occidentalis (western predatory mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Phytoseioidea; Phytoseiidae;
OC Typhlodrominae; Galendromus.
OX NCBI_TaxID=34638 {ECO:0000313|Proteomes:UP000694867, ECO:0000313|RefSeq:XP_028969161.1};
RN [1] {ECO:0000313|RefSeq:XP_028969161.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_028969161.1; XM_029113328.1.
DR AlphaFoldDB; A0AAJ7WJH8; -.
DR GeneID; 100907162; -.
DR KEGG; goe:100907162; -.
DR Proteomes; UP000694867; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; IPR016187; CTDL_fold.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_028969161.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694867};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1186
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042493073"
FT DOMAIN 889..927
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 961..1126
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 104..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..814
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 125002 MW; 1F2F48632D2216A2 CRC64;
MISGWSLVKT YLILIVSQGV LDSLKFYSFN SHAPAEVLCD DTFLVLGNGD IHENERSESG
SVIDDSQLTD GSGDDLENYV PLKKHDKSLF KIFGAVKHQE LLHQEQKEKP EHHHERHHRH
HQHHHRHQGA GAADLENTGL FDDNNSNNNN QVAESSPVIA SVASKDESFG KIDGESATAN
GLENASDMLD AEISLVSQND TDVGDYHTLL STTVFSSTSE QPTTFVVDDK AVPTDVTETP
LGNASELLAG VDIQEHVLDS FAVLHIDEDI RGDYSGNGEE LDSENRLDTA KESETALPDD
VEVRADLGSG QGSEAVKNGD TTKSNEEIGG SRVEATREAD DEVSRRDEEV EKMLEAEGVA
SSTIEHHVAK ETVCNPEILA DWITKDRLGI REKLRGPPGN CSCNPVYDIE SLRGPRGLNG
RDGMDGSPGH PGLPGPEGAR GEMGLPGPEG PQGPQGPTGP MGPQGEKGDG GSDGVPGMQG
PQGPPGPPGP PGPSHGRYFD FDTGLGDGTY GTYMGAPGPA GPIGPQGPAG AKGSRGPPGE
KGAKGDTGSK GSRGLRGPMG ITGRQGAKGE PGMNGADGRP GTPGFTGDKG ERGERGEPGV
GLPGPPGPPG RSVVSHDDYD NGLILEATKG DRGEMGPPGP QGIDGRTGPR GEPGEPGPAG
PQGPKGEPGP VTMLGDNVAI HVMKGDKGDE GRRGKRGYRG PPGPAGGPPG PAGPPGPPGE
GLKGERGEPG PPGLVTSADG EVIRGERGEP GPQGPQGEIG PLGPKGDRGD RGSPGPPGPV
TFSDGSSFDV ATIKGEKGEP GVGIQGPQGV GLRGPQGPPG PPGPPGPSSW NPDFNPNAPV
SAMLRAPGSM LSHFKGPPGP PGPPGECVCN PKSSQVVPGA LVVKDQKSLH ETTDFTSPGA
IAYVTDDENL MVRVPQGWQY VGLGPIILPT VTTTTTTTEQ PKPQFTSDDL KNVPTKRRKI
RMAALNQPYS GDMHGVRSAD YECYRESRNA GLNGTFRAFL ASRIQNVESL VRARDASAPV
VNLKGELLFN SWREIFSGSL GHFPISPRIY SFDGKNVMNE HTWPQKIVWH GADRNGARNM
EHYCDAWNSA ASRKTGLGSS LLHNRLLDQQ KYPCNMRFIV LCVEISSSSS AVPVASHSKD
QESRWRRRGR SLHDDTPSSD HLLSFEEYSD SLDRKKKSWS DDELHL
//
