ID A0A8B8HQR0_VANTA Unreviewed; 1079 AA.
AC A0A8B8HQR0;
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 X3 {ECO:0000313|RefSeq:XP_026486887.2};
GN Name=LOC113393962 {ECO:0000313|RefSeq:XP_026486887.2};
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_026486887.2};
RN [1] {ECO:0000313|RefSeq:XP_026486887.2}
RP IDENTIFICATION.
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_026486887.2};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_026486887.2; XM_026631102.2.
DR AlphaFoldDB; A0A8B8HQR0; -.
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..1079
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5046057195"
FT DOMAIN 794..839
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 877..1048
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 237..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 115184 MW; CB16A81DAD46D322 CRC64;
METLNWIVRI NLILLIGCLS ELHTDTVKYE YDILSKVLNT ITPTSYSSVN GTDIYGAIKL
ITNDPISVSL DKFEIKDDKL VTPFEIYALV NFNKVISSCL FNIKAGDDNK LSLCVEKVDE
KIVKLILSSS TVDTNIQILY DIEENSWSNI LLRVEENKLR LYNNCAIFDE QLYSSIEKPL
REIEIPKNAK LYLGKLDKND KRLFEGSIQS LKIFPNPEFY GRRDICDDGF KLPDSKDDYA
SSHSDFTDST 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
//
