ID A0A9C6WEN3_DROAB Unreviewed; 1022 AA.
AC A0A9C6WEN3;
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 X5 {ECO:0000313|RefSeq:XP_051860248.1};
GN Name=LOC117567544 {ECO:0000313|RefSeq:XP_051860248.1};
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_051860248.1};
RN [1] {ECO:0000313|RefSeq:XP_051860248.1}
RP IDENTIFICATION.
RC STRAIN=15112-1751.03 {ECO:0000313|RefSeq:XP_051860248.1};
RC TISSUE=Whole Adult {ECO:0000313|RefSeq:XP_051860248.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_051860248.1; XM_052004288.1.
DR AlphaFoldDB; A0A9C6WEN3; -.
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_051860248.1};
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..1022
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039699343"
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 986..1006
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 1022 AA; 108277 MW; BA8468DC62E93E26 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 PPLLNTPTFT TAPEYETWYP RMLRVAALNE PYVGDLQGIR GADFACYRQG
RRAGLLGTFK AFLSSRVQNL DSIVRPADRD LPVVNTRGDV LFNSWKGIFN GQGGFFSQAP
RIYSFSGKNV LTDPLWPLRL VWHGSLPNGE RSMDTYCDAW HSGSHEKFGY ASNLLGNKLL
DQERQPCDGK LIVLCVEALS QDRRKKRDLS SPHSHSHSRS RHSELEFSTA EEYGEYLDNL
LL
//
