ID A0A9C6WEN5_DROAB Unreviewed; 1008 AA.
AC A0A9C6WEN5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X7 {ECO:0000313|RefSeq:XP_051860249.1};
GN Name=LOC117567544 {ECO:0000313|RefSeq:XP_051860249.1};
OS Drosophila albomicans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7291 {ECO:0000313|Proteomes:UP000515160, ECO:0000313|RefSeq:XP_051860249.1};
RN [1] {ECO:0000313|RefSeq:XP_051860249.1}
RP IDENTIFICATION.
RC STRAIN=15112-1751.03 {ECO:0000313|RefSeq:XP_051860249.1};
RC TISSUE=Whole Adult {ECO:0000313|RefSeq:XP_051860249.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_051860249.1; XM_052004289.1.
DR AlphaFoldDB; A0A9C6WEN5; -.
DR GeneID; 117567544; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000515160; Chromosome 3.
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 CDD; cd00247; Endostatin-like; 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
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_051860249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000515160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1008
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038745045"
FT DOMAIN 37..225
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 252..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..517
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 106503 MW; 6BD6BD9A88AF0ADB CRC64;
MRSLLLVLWL AVPHLIAVLG ALEPELDDSN ETDKFGEHRL TDIITDEHYP SIKFGEGEDG
FPAFNFFSTA DVKSYSKVLL PQKLADFAIQ NTYKLSSLKG GYLFSVLRSM DDKVVQLGVH
LSPVIKNSYN VTLFYAQPDQ NDNVKIASYP IVHVPDKWNS IAFQVFSDNV VFFYDCKAVN
TTAIVRDPFE LSFASSSVLY IAQAGSQLGG NFEGFLQNIY LYTNPDAITM QCTAPPKPTV
ALQPDLDNEL TLDSKSESDV LSDTEVDTNS STDDSTADEN DLSNPEFWAG ATDNYDSSDL
QPPGQTEYML ERSHRGIKGE KGDRGPKGDS IRGPPGPPGP PGPKGETPVY PPFVETPSAG
AKYTGECTCN ATDILEAIKD NETLRETLRG PPGTQGRDGK TGAPGLTGAT GVTGARGPEG
IQGEKGEPGV DGMPGVMGPP GPPGAPGLPE SYDESLMGNS MGSLRSSTAT QAGPKGTTGD
KGEPGRPGDR GEKGHKGAHG PTGPKGEPGA PGLPGLAGQP GDGNGTKGER GEKGEKGMRG
RRGGTGAAGP IGPPGKPGPT GDIGHSGRPG ATGPKGDAGL KGAKGDAGGR EGAKGEKGDR
GSDGRDGLPG PPGLPATAGA GDGDSGGVQY IPMPGPPGPP GPPGLPGLSI TGPKGEAGMD
SRGSFFGDAS YYGRPEPPSQ KAHSHKHGDS MGEGEELPHL SASSSNMNMR IVPGAVTFQN
IDEMTKKSAF SPPGTLAYIT EEEAMLVRVN KGWQYIALGT LVPIATPAPP TTVAPSLRFD
LQSKNLLNSP PPLLNTPTLR VAALNEPYVG DLQGIRGADF ACYRQGRRAG LLGTFKAFLS
SRVQNLDSIV RPADRDLPVV NTRGDVLFNS WKGIFNGQGG FFSQAPRIYS FSGKNVLTDP
LWPLRLVWHG SLPNGERSMD TYCDAWHSGS HEKFGYASNL LGNKLLDQER QPCDGKLIVL
CVEALSQDRR KKRDLSSPHS HSHSRSRHSE LEFSTAEEYG EYLDNLLL
//
