ID A0A6P8TUA8_GYMAC Unreviewed; 1253 AA.
AC A0A6P8TUA8;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|RefSeq:XP_034061980.1};
GN Name=LOC117539778 {ECO:0000313|RefSeq:XP_034061980.1};
OS Gymnodraco acuticeps (Antarctic dragonfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Gymnodraco.
OX NCBI_TaxID=8218 {ECO:0000313|Proteomes:UP000515161, ECO:0000313|RefSeq:XP_034061980.1};
RN [1] {ECO:0000313|RefSeq:XP_034061980.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR RefSeq; XP_034061980.1; XM_034206089.1.
DR AlphaFoldDB; A0A6P8TUA8; -.
DR GeneID; 117539778; -.
DR Proteomes; UP000515161; 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 FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 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; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000515161};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1253
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028342544"
FT DOMAIN 37..225
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 224..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..363
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..383
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..565
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..779
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 128711 MW; A2579D7EFAE250E6 CRC64;
MTSRIPPWFF GIFLLVLRFC SHRSSAQLLE DRGSPGALDL TELIGVPLPP SVSFVTGFEG
YPAYSFGPDA NVGRLTKSFI PDPFYYNFAI TVTAKPTTRQ GGMLFAITDA YQKIVHLGIA
LSEVEDGSQR VVLYYTDPGT GRTQEAASFK MGDMTGRWAR FSLTVQGAEV RLYMDCEEYH
RVAFSRSPQP LTFEPSSGMF IGNAGGTGLQ RFVGSIQQLV LKSDPTAPDD QCEEDDPYAS
GYGSGDDAYD DLEGRDEVKK IVNTMPLPEL DPSYSAPVRA PPTEMSRAFV DDDDEDIEET
SGQEVEKTTV IVKSSPTVTP ASIRDTSLQV SSGQKGEQGE PGPSGPPGPP GTASGGGEGG
EPGPRGPQGP AGPSGKPGAS GKDGQAGSKG ETGAQGATGV PGFPGLEGDS GPIGEKGDPG
LGRPGPPGPP GPPGPTSKSS MFLEGSGGLE DFDSDAEIMR GPPGPPGVPG PPGAQSENTF
PGSPGAPGKD GKDGQRGEPG VPGVDGKDGD PGSAGENGDK GEPGVNGQPG TKGDQGPAGF
PGQPGSEGPE GHPGPPGAPG PPGPPGRGYS MDFEDLEGSG MQGGFGSALS RGPEGPAGVP
GIQGPRGKDG LDGAAGKPGE RGEKGATGSP GFPGLDGFKG EEGLKGDKGQ KGEVGRDGLS
IPGPPGPPGP SGPLINLQDL QLNDTDGTFN FSGISGPQGP KGDGGLPGVQ GPPGMKGERG
EPGLVLADDG LMLSGLAAAP GVKGDHGLPG PVGIQGPTGP SGPKGEFGFP GRPGRPGRMG
LKGERGDAAG LPGLPGPAGL PGRPGIFNCP KGTVFPLPPR PHCKQTSGAM MALNLSCMMH
VHSGKLKAHC KYIQKRNPDG TVAVGNCQTG YKGERGERGL PGLPAPQSSF LSRGGWGSSG
DQGLQGEKGD RGEGGFSGTP GTPGRTGPVG PKGESVIGPQ GPPGVPGSPG FPGYGRPGPV
GPAGPPGPPG PSGTPLRYGS ALTVAGPPGP PGPSGPSGSS SSMKTFTSRE SMMQHTVRDA
EGTMAYVTST GSLFIKVSQG WKEIQLGSLI YLSNNIIPQD EPRIAYQIRG ETMERIRSVN
ERLTLVALNQ PHSGHMTGLD TADRLCYEQA KAMGLAPNYR AFISSNRQDL VHVVYPGFRE
NLPVTNLRGD VMFRNWREIF TGDGGPLDAR IPLYSFDGRD VIADPFWPQK SMWHGSSSRG
LRVVDKHCET WRADHLSVMG QSSSLTSGLL LGQQTRSCSN QYIVLCIETH KTL
//
