ID A0A9C6SVV2_DROAB Unreviewed; 1002 AA.
AC A0A9C6SVV2;
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 X8 {ECO:0000313|RefSeq:XP_051860250.1};
GN Name=LOC117567544 {ECO:0000313|RefSeq:XP_051860250.1};
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_051860250.1};
RN [1] {ECO:0000313|RefSeq:XP_051860250.1}
RP IDENTIFICATION.
RC STRAIN=15112-1751.03 {ECO:0000313|RefSeq:XP_051860250.1};
RC TISSUE=Whole Adult {ECO:0000313|RefSeq:XP_051860250.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_051860250.1; XM_052004290.1.
DR AlphaFoldDB; A0A9C6SVV2; -.
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_051860250.1};
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..1002
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038735882"
FT DOMAIN 37..225
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 239..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..471
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 106165 MW; 1683EFD5FC22F5CE 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
ALQPATDNYD SSDLQPPGQT EYMLERSHRG IKGEKGDRGP KGDSIRGPPG PPGPPGPKGE
TPVYPPFVET PSAGAKYTGE CTCNATDILE AIKDNETLRE TLRGPPGTQG RDGKTGAPGL
TGATGVTGAR GPEGIQGEKG EPGVDGMPGV MGPPGPPGAP GLPESYDESL MGNSMGSLRS
STATQAGPKG TTGDKGEPGR PGDRGEKGHK GAHGPTGPKG EPGAPGLPGL AGQPGDGNGT
KGERGEKGEK GMRGRRGGTG AAGPIGPPGK PGPTGDIGHS GRPGATGPKG DAGLKGAKGD
AGGREGAKGE KGDRGSDGRD GLPGPPGLPA TAGAGDGDSG GVQYIPMPGP PGPPGPPGLP
GLSITGPKGE AGMDSRGSFF GDASYYGRPG ARSSLDELKA LRELQDLRDR PDGTAEPPSQ
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
//
