ID A0A6P8TC13_GYMAC Unreviewed; 1630 AA.
AC A0A6P8TC13;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X1 {ECO:0000313|RefSeq:XP_034061368.1};
GN Name=LOC117539332 {ECO:0000313|RefSeq:XP_034061368.1};
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_034061368.1};
RN [1] {ECO:0000313|RefSeq:XP_034061368.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_034061368.1; XM_034205477.1.
DR GeneID; 117539332; -.
DR KEGG; gacu:117539332; -.
DR InParanoid; A0A6P8TC13; -.
DR OrthoDB; 10060752at2759; -.
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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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; 2.
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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1630
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028006610"
FT DOMAIN 120..309
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 27..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..105
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..830
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..914
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..938
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 169660 MW; E28C38D0246CC60A CRC64;
MLRMKTLLLL LAFFAWSSDA WFWSKDPEPT TSTSIESTPS GTTGAANATQ KNLEEEEEEE
EEEEEEDDNL SGVGDEILNV TTGIRKFVAA WDVTPTPGTT NGGPTQKVES ANPNTTEESG
VSLLQLIGDP PPDEIPRVTG PRGEPGFIFN RASVSGQLAL AHIPNPFHRH FSLVFHIKPT
SPDASVLFSI TDGPQKIMYV GVKLSAVQNS RQRVQFFYTE PGSEASYEAA SFEVPSMVET
WSRFSLSVFD EQVTFYQGCD SEPQVVKFER SPDPMELDAG AGIFVGQAGG ADADKFKGVI
LDLKVVGDHR AAERLCDDED DSDAASGDFG SGDGERRQTG HTVKTTPRPL RPVPAPPLIP
SQGNILRESG TAVSKGEKGD RGNQGLKGDL GPAGPKGESS SSGSSSGSSS QGGGQKGEKG
VKGSSGFGYS GNKGERGAQG SSGPPGPPGP AAEVVRLGNG DVVQQVSGPS GPPGFPGING
AQGPAGTDGE PGDPGEDGKA GATGPQGSPG NPGTAGFKGE KGDVGEGQPG PRGAPGPPGL
PGTGTGDHPT FFDMEGSGFP DSDKIRGGRG LPGLPGPPGP PGTSVALGPN GPVAFGPPGP
PGQDGVPGIP GPPGQPGRPG LPGPGGERGE GGDLGLPGVA GEKKNSEDSG FFTGLYSYFA
PSSTGSQGDL GLPGTSGQSG LAGLPGPMGP VGPVGPPGPP GPGYRGSHSN QDQDDVNNGY
AGLPGPPGPQ GPYGIAGLPG KSGLPGNHGD KGTEGSRGPP GMPGMDGFPG QSGDKGDRGQ
RGEQGLPGRD GGGAGPPGPP GPPGEITYQR SDSNEVIWNG GSQGGSGLPG QAGFPGPSGP
KGDKGDTGLP GYAAKGAKGE PGIVLGPDGR PQYLGGLAGR PGDAGPPGPE GPSGPYGASG
HKGEIGIPGR PGRPGLNGVG GEKGDSGSGS GSGVGYPGVP GAPGPPGPPG SYPTDRQGGY
DDYSRYNPAA KGDKGDPGPP GRVEITGGGS TFDIYSLRNE MKGESGTPGY KGDKGEPAGG
YYDPRYEVSG AGAPGPPGPR GDSIVGPAGP QGPPGEPGRG YDGQQGPPGP PGPAGGSTPE
VYRGTQTINI PGPPGPPGTP GLPGYSSGVT VLRTYDTMTA TARRQPEGSL VYIIDQTDLY
LRVRGGIRQV QLGDYIALPV VDGNEVAAVE PPPVVPYSPH HTENTDPSVH DSQRQPESPV
YPDPHHPTHQ DPHHPTRQDP HHPTHQDPHH PTHQDPHHPT HQDPRHPHEP THQDPHEPTH
QDPHHPTHQD PHHPTHQDPR HPHEPTHQDP HHPTHQDPHH PTHQDPHQPT HQDPHQPTHQ
DPHHPHQPTH QDPHHPHQPT HQDPHHPTHQ DPHHQEPQYP SNPDPRYPSH PDPRYPSNPD
PRYQPDPRFP PPTDPRFPSY TDRLNQPDGR VSVNTAQERP AYPDSRYADP RFAVTPQRRP
PPRVPHTPVH HHTSGAGLHL IALNSPHSGS MRGIRGADYQ CFTQAQAIGM KGTFRAFLSA
KLQDLHSIVR RSDRDHLPIV NLKDEVLYDS WDAMFNEGRM KDNVPMYSFD GKDVLNDSTW
PEKMLWHGSN AAGRGQVDSI CEGWRVGEQA LTGTAAELRS GNLLQQTPSS CSGSYVVLCI
ENSYIGQAKR
//
