ID A0A6I8VJS7_DROPS Unreviewed; 1023 AA.
AC A0A6I8VJS7;
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(XV) chain isoform X8 {ECO:0000313|RefSeq:XP_015042759.2};
GN Name=Mp {ECO:0000313|RefSeq:XP_015042759.2};
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_015042759.2};
RN [1] {ECO:0000313|RefSeq:XP_015042759.2}
RP IDENTIFICATION.
RC STRAIN=MV-25-SWS-2005 {ECO:0000313|RefSeq:XP_015042759.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015042759.2};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_015042759.2; XM_015187273.2.
DR AlphaFoldDB; A0A6I8VJS7; -.
DR Proteomes; UP000001819; Chromosome X.
DR ExpressionAtlas; A0A6I8VJS7; baseline.
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 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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_015042759.2};
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..1023
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026073670"
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..693
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 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"
SQ SEQUENCE 1023 AA; 107974 MW; 2260E933E4AAC86C 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 GDASYYGRPE APRQPGHSHK HEEALGPAVG EEPYFSASSS NINMKIVPGA
VTFQNIDEMT KKSALNPPGT LAYITEEEAL LVRVNKGWQY IALGTLVPIA TPAPPTTVAP
SMRFDLQSKN LLNSPPPPLN TPTWYPRMLR VAALNEPSVG DLQGIRGADF ACYRQGRRAG
LLGTFKAFLS SRVQNLDSIV RPADRDLPVV NTRGDVLFNS WKGIFNGQGG FFSQAPRIYS
FSGKNVMTDP LWPLKMVWHG SLPNGERSMD TYCDAWHSSA HDKSGYASDL AGHKLLEQKR
QPCDGKLIVL CVEALSQDRK RKKRDASDSH SYGHSHSRGP SRSQNLEFRT AEEYAAHLDD
LLL
//
