ID A0A6I8W5E4_DROPS Unreviewed; 1023 AA.
AC A0A6I8W5E4;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X9 {ECO:0000313|RefSeq:XP_033238563.1};
GN Name=Mp {ECO:0000313|RefSeq:XP_033238563.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_033238563.1};
RN [1] {ECO:0000313|RefSeq:XP_033238563.1}
RP IDENTIFICATION.
RC STRAIN=MV-25-SWS-2005 {ECO:0000313|RefSeq:XP_033238563.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_033238563.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_033238563.1; XM_033382672.1.
DR AlphaFoldDB; A0A6I8W5E4; -.
DR Proteomes; UP000001819; Chromosome X.
DR ExpressionAtlas; A0A6I8W5E4; baseline.
DR GO; GO:0005587; C:collagen type IV trimer; 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 CDD; cd00247; Endostatin-like; 1.
DR FunFam; 2.60.120.200:FF:000137; Multiplexin collagen isoform Ap3; 1.
DR FunFam; 3.10.100.10:FF:000048; Multiplexin collagen isoform Ap3; 1.
DR FunFam; 3.40.1620.70:FF:000001; Multiplexin collagen isoform Ap3; 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1098; MULTIPLEXIN, ISOFORM R; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_033238563.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1023
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026206894"
FT DOMAIN 32..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 247..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..552
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 108072 MW; DA8FEAD2A4D3A385 CRC64;
MRLLLLMLGL VWTFLAPARC SFDLIGQSIK DALAEYTLTD IMNNNQFAGI EFGEAEDGFP
AFRFLQTADV KSPYRMLLPE KLYEFAILIT YRQSSLKGGY LFSVVNPLDT VVQLGVHLSP
VVKNSYNVSL VYTQADQSIG RKLASFSVAH VADKWNSIAF QVLSDRVSFY YDCELRNSTP
VTREPIELVF DSASTLYIGQ AGSIIGGKFE GYLEKINVYG NPDAINVTCM PPPKATAAPT
AAATDIFDAS GMQPPGQTQY THERPYRGIK GEKGERGPKG DSIRGPPGPP GPPGPKGEAA
AYPPFVETTS AGAKYTGECT CNASDILEAI KDNESLRETL RGAPGTQGKD GKPGTPGHTG
ATGVPGARGA RGSEGAQGQK GEPGVDGLPG VAGPPGPAGP PGLPENYDIN WNPTRTFKES
LMVNSMGTFR GTTQPGPKGV SGEKGEAGQK GERGDPGHKG AHGSNGAKGE PGEPGTPGLP
GLPGQAGQPG GLEGLSANGT KGEKGEKGMR GRRGGTGSTG PIGPPGKPGA MGDIGHSGRP
GMTGPKGEMG PKGPKGDTGG REGPKGDKGD TGQDGRDGLP GPPGLPASGG GDGDSSGVQY
IPMAGPPGPP GPPGLPGLSI TGPKGEPGMD SRSFFGDASY YGRPGARSSL DELKALRELQ
DLRDRPDGTA EAPRQPGHSH KHEEALGPAV GEEPYFSASS SNINMKIVPG AVTFQNIDEM
TKKSALNPPG TLAYITEEEA LLVRVNKGWQ YIALGTLVPI ATPAPPTTVA PSMRFDLQSK
NLLNSPPPPL NTPTFTTAPE YETWYPRMLR VAALNEPSVG DLQGIRGADF ACYRQGRRAG
LLGTFKAFLS SRVQNLDSIV RPADRDLPVV NTRGDVLFNS WKGIFNGQGG FFSQAPRIYS
FSGKNVMTDP LWPLKMVWHG SLPNGERSMD TYCDAWHSSA HDKSGYASDL AGHKLLEQKR
QPCDGKLIVL CVEALSQDRK RKKRDASDSH SYGHSHSRGP SRSQNLEFRT AEEYAAHLDD
LLL
//
