ID A0A8B7PQC6_HYAAZ Unreviewed; 1202 AA.
AC A0A8B7PQC6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_018027671.1};
GN Name=LOC108682925 {ECO:0000313|RefSeq:XP_018027671.1};
OS Hyalella azteca (Amphipod).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Peracarida; Amphipoda; Senticaudata;
OC Talitrida; Talitroidea; Hyalellidae; Hyalella.
OX NCBI_TaxID=294128 {ECO:0000313|Proteomes:UP000694843, ECO:0000313|RefSeq:XP_018027671.1};
RN [1] {ECO:0000313|RefSeq:XP_018027671.1}
RP IDENTIFICATION.
RC TISSUE=Whole organism {ECO:0000313|RefSeq:XP_018027671.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_018027671.1; XM_018172182.1.
DR AlphaFoldDB; A0A8B7PQC6; -.
DR GeneID; 108682925; -.
DR KEGG; hazt:108682925; -.
DR OMA; HKMVWHG; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000694843; Unplaced.
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 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1071; COLLAGEN ALPHA-1(VII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_018027671.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000694843};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 664..709
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 889..1050
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 136..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..452
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..595
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..795
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 125045 MW; D7CE96207B9BB8B0 CRC64;
MAAGLSRSSG LVIALVLVVV LALVAVISAG AAFGWYDDEP RAVEALEQNG MLNAGRPNRF
EGLHGKAANG LTERGRGDDF NYYDDRTSGL FVPLSEWSGA GGGMTGGPMT GGPMGDTALG
QCRCNTSHLL NLVTAHIPRG PPGIRGRDGK PGAPGLSGNP GTQGERGMPG RSGDKGERGE
VGPQGKEGLQ GPKGEPGTDG QQGPVGPPGP PGPPGNPGIA MGRGDHGLGG RKPSWGNGIG
YSMTSMDGMA ETTSVEAIGM PGVMGPPGPP GLPGAPGLPG LKGAEGPKGE RGYEGMKGNK
GNEGIQGPAG RLGDKGTRGP PGIDGIPGRP GLDGMVGLKG QKGDPGPTGV GRPGPRGPKG
IKGSQFYSPE EVNAMVMSTI QRFTDMTPEG PQQLRDVSKK VEVFLPKGEP GEPGMPGLMG
LKGEEGPMGP IGPQGPTGNM GPRGEPGSSG EAGEPGDKGA KGETGPPGPV SFSNGTVVVI
KGQKGDAGGD GEAGRRGLRG LMGPPGPRGP PGPPGGIEGF DGDVGGIKGQ KGEQGPPGPP
GPGAVGGMGR GATYVDGGLF GIVARPGKKP GFSGVFGADE TGDIGTAGLG SGIAGPPGPP
GPAGPRGPPG PPGPPGGDSY SGHNTMPIPG PPGPPGERGA PGIPGGISSD AGYGLPLTTS
STITFTSRTS MIQDWTSYSV GSLAYVIADD SMFARTSRGW REIMLGTVLT DASESQGMRP
LPPVGGNVPE ILHGRRNKPS WQPSPWGDPM IQSKDRNINQ RGPPNVHEHQ PTSHHDRTSH
ERHNGHGSGH SKHGSGHNGH GSGRNGHGSP GNGHGSSMDT DTRLPLGQDY FYDSRDRSDY
GHQSYNHDHT YHEHPGPEPS PDYETDEGGW RPTQTPLGEN WGSSSGEHLR VAALNEPVSG
DMKGQKAADF SCYRQARSAG LTGSFRAFLA DSSGITSLVR STLQNLPLVN LRGETILSSW
QDLSLTGGLF LEAPKIYSFD GQNVAESERW PNKYVWHGAT RRGEKADNCN AWTSSAAMRV
GHASSLQSMQ LLAQEKISCD NPLVVLCVET NLPKRRKRSL TKRSIENLEA ERANETIIHG
DSFVWVTEAS QGKKRLQESI DDGNFMVTKN RVKASQFSNN ESKFSIQPNY KALNNDLSSD
EDSNERSMNK KFFRSFNSTS EPEKSGHLPN LDLNAQSHRD EARRKTVNKK IFEMMDLMEE
ED
//
