ID A0A6I8VKD3_DROPS Unreviewed; 1056 AA.
AC A0A6I8VKD3;
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 X2 {ECO:0000313|RefSeq:XP_015042765.2};
GN Name=Mp {ECO:0000313|RefSeq:XP_015042765.2};
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_015042765.2};
RN [1] {ECO:0000313|RefSeq:XP_015042765.2}
RP IDENTIFICATION.
RC STRAIN=MV-25-SWS-2005 {ECO:0000313|RefSeq:XP_015042765.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015042765.2};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_015042765.2; XM_015187279.2.
DR AlphaFoldDB; A0A6I8VKD3; -.
DR Proteomes; UP000001819; Chromosome X.
DR ExpressionAtlas; A0A6I8VKD3; 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_015042765.2};
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..1056
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026339235"
FT DOMAIN 32..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 282..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..587
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 111655 MW; B879453FAEB56915 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
AADLDSFLDE GSGAGEPFEE STELNILSDD FWSSADEATD IFDASGMQPP GQTQYTHERP
YRGIKGEKGE RGPKGDSIRG PPGPPGPPGP KGEAAAYPPF VETTSAGAKY TGECTCNASD
ILEAIKDNES LRETLRGAPG TQGKDGKPGT PGHTGATGVP GARGARGSEG AQGQKGEPGV
DGLPGVAGPP GPAGPPGLPE NYDINWNPTR TFKESLMVNS MGTFRGTTQP GPKGVSGEKG
EAGQKGERGD PGHKGAHGSN GAKGEPGEPG TPGLPGLPGQ AGQPGGLEGL SANGTKGEKG
EKGMRGRRGG TGSTGPIGPP GKPGAMGDIG HSGRPGMTGP KGEMGPKGPK GDTGGREGPK
GDKGDTGQDG RDGLPGPPGL PASGGGDGDS SGVQYIPMAG PPGPPGPPGL PGLSITGPKG
EPGMDSRSFF GDASYYGRPG ARSSLDELKA LRELQDLRDR PDGTAEAPRQ PGHSHKHEEA
LGPAVGEEPY FSASSSNINM KIVPGAVTFQ NIDEMTKKSA LNPPGTLAYI TEEEALLVRV
NKGWQYIALG TLVPIATPAP PTTVAPSMRF DLQSKNLLNS PPPPLNTPTF TTAPEYETWY
PRMLRVAALN EPSVGDLQGI RGADFACYRQ GRRAGLLGTF KAFLSSRVQN LDSIVRPADR
DLPVVNTRGD VLFNSWKGIF NGQGGFFSQA PRIYSFSGKN VMTDPLWPLK MVWHGSLPNG
ERSMDTYCDA WHSSAHDKSG YASDLAGHKL LEQKRQPCDG KLIVLCVEAL SQDRKRKKRD
ASDSYGHSHS RGPSRSQNLE FRTAEEYAAH LDDLLL
//
