ID A0A8B8HQJ5_VANTA Unreviewed; 1069 AA.
AC A0A8B8HQJ5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X6 {ECO:0000313|RefSeq:XP_026486890.2};
GN Name=LOC113393962 {ECO:0000313|RefSeq:XP_026486890.2};
OS Vanessa tameamea (Kamehameha butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Nymphalinae; Vanessa.
OX NCBI_TaxID=334116 {ECO:0000313|Proteomes:UP001652626, ECO:0000313|RefSeq:XP_026486890.2};
RN [1] {ECO:0000313|RefSeq:XP_026486890.2}
RP IDENTIFICATION.
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_026486890.2};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_026486890.2; XM_026631105.2.
DR AlphaFoldDB; A0A8B8HQJ5; -.
DR GeneID; 113393962; -.
DR Proteomes; UP001652626; Chromosome 16.
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 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; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF966; COLLAGEN ALPHA-1(XXII) CHAIN-LIKE; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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 Reference proteome {ECO:0000313|Proteomes:UP001652626};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1069
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5045867151"
FT DOMAIN 784..829
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 867..1038
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 236..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 114078 MW; F6B5CDDA1BC5A020 CRC64;
METLNWIVRI NLILLIGCLS ELHTDTVKYE YDILSKVLNT ITPTSYSSVN GTDIYGAIKL
ITNDPISVSL DKFEIKDDKL VTPFEIYALV NFNKVISSCL FNIKAGDDNK LSLCVEKVDE
KIVKLILSSS TVDTNIQILY DIEENSWSNI LLRVEENKLR LYNNCAIFDE QLYSSIEKPL
REIEIPKNAK LYLGKLDKND KRLFEGSIQS LKIFPNPEFY GRRDICDDGF KLPDSFTDST
AIEDESDDES EIDSLERVEK CDKGEKGDTG DKGEKGDKGE SITGPIGSPG PPGPEGPQGL
PGKKGDEGSC QCSEKVVSSL LLTMPAMRGP PGEPGPQGED GEQGRPGLTG LIGKQGERGP
EGLKGDQGNR GEDGIPGRDG EQGTKGEPGK DGNPGPPGPV GPIGPPGPPG PVYKEIEEAK
VPVADERGET GPIGPPGTPG HDGMKGEKGD QGMKGEKGEE VTKIITHRGL DGEMGPRGEK
GDTGKAGKNG IPGVPGTHGH SGEKGEKGDK GDRGDIGLPG LPAKLSSILD TDIDPLENAE
IIEKLRGYKG DRGVAGHKGD KGELGPIGPT GLPGSIGPQG PQGERGPHGH NGESGPIGPR
GYKGEPGEPG PPGNVPTSAI SLMKGPPGKP GPRGPIGHTG KRGPTGPPGP KGPKGQRGDT
GIQGEAGPKG DVGIMGPKGE KGEVPYIDVK KLKGEKGDTG EAGKSGEPGK PGSPGTCEDS
NSIIVPGPPG PPGPPGRPGV SITGPKGEPG GILTRSTLYA FGNKNGGADT SNEDDDFYTA
ATIIYKSSTA LLKRTSITPL GTLAYILEEN ILLMRVENGW QYIIMGSFLQ TRESHTSTTP
RPKYYNPPAT STSPPLRDAP YTDNYIRLVA LNEPYPGNMV TSINRTGRSA ADQECYNQAK
NSQQPSSFVA FLANKVEDLR SIVKRLRDRN VPVVNLYGDV LFDSWSNMFN GSGALLAKSN
IYSFSGKNVL IDPTWPIKAV WHGGNSFGIR TPRTYCEEWQ SDSPLSIGAA SSLKSNRLLE
QEQYSCDNKL IVLCVEATTN AHRHIRHAHP KSRRRLENYE KFDNRIPRL
//
