ID A0A6P8SVI5_GYMAC Unreviewed; 1410 AA.
AC A0A6P8SVI5;
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, type XV, alpha 1b isoform X5 {ECO:0000313|RefSeq:XP_034054974.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_034054974.1};
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_034054974.1};
RN [1] {ECO:0000313|RefSeq:XP_034054974.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_034054974.1; XM_034199083.1.
DR GeneID; 117534843; -.
DR CTD; 558137; -.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 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; 3.
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 ECO:0000313|RefSeq:XP_034054974.1};
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..1410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028189536"
FT DOMAIN 139..328
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 329..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..478
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..629
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..960
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1080
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1112
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1193
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 144277 MW; C105CCC69E49E4C7 CRC64;
MGALRLSFAL FFLSFSPAQA QWWSFIWAKP KTTTISMTSP IPSYITSPSI TSLGSSDIPG
TAEWMLKEDR VTEKAPEIST LTEGSVLPPT PTPGVEIFGQ STAVPGTLPP KENAGAGSKA
RAQCKLLKHW KSERGSGGHL DLTELIGVPL PPSVSFTPGH EGFPAYNLGP DANIGRLTKT
FVPGSFYRDF AIIVTVRPAS QRGGVLFAIT DARQKVVELG LALTPVRGGL QSILLYYTDE
EQASHSHKAA SFSVPDMTEQ WTRFTVVVEQ DEVRLYMDCG EAERTTFHRR PKRLNFSHNS
GVFVANAGGT GLDKFVGSIQ QLVIKDDPRA AEEQCEDDDP YASGFTSGDD ALDDRESEEE
MMKNTHERKQ GTEKEEGSVP VRAPPTEAPE VELEEFSGQQ TTTEATEDML LKGPHMTQEP
GEEPRDGHVR HGIKGERGSP GPRGPPGHPG PTPLPGQAQP GPRGTQGPAG APGSPGQQGR
DGQAGHKGDK GDAGQRGTQG LSGSDGEAGS KGEKGDQGVG APGLPGPPGP PRSHSVSYGA
DALGSGFEDL DSDTELIRGH PGLPGPPGPP GPPGPLPSSS AEGFSSGYAG LPGKDGPQGK
PGLPMYEDWF SGSGSDASGL SSEFSSDLGS GFSSGFSSDP GFASGSGLDF GSAWGSGEGL
AGRNGSPGLS GALGEKGEQG LAGQPGPKGE CGSLGTNGSS GAPGPSGPPG KRGPSGPPGP
PGPPWPTKFF VEDMEGSGKS DMLIGTGVRG TQGPPGIHGP TGPKGEDGAT GAPGLSVKGE
PGGKGPEGRQ GPAGLPGARG AKGEKGNLGS KGDRGVDGLS IPGAPGPPGP PGPTINLPDL
LLNMTDGIFN FTDIRGPPGA VGPEGLPGRA GFPGPRGPKG DVGPAGVQGP LGLKGEKGEP
GVTIAADGSL ISAPRGPQGP KGLKGDRGFS GPAGLMGPIG PNGQKGEYGF PGRPGRSGMP
GRKGDKGDAV GLSGPPGPPG QPGLPGRVVG LKGSGTARDS VGAKGNKGDI GIPGEPGTPA
PEFPDGVVGA RGDKGYQGQK GDKGEGLPGP PGLPGRSGLV GPKGESIVGP HGPVGPVGEP
GAPGFGRPGP RGPPGPAGPP GPASGYGSGA SVPGPPGPQG PTGSPGNANA MTVYKTSNAL
GRETHRVAEG TLAYVSEKGG ELFIRARNGW RKIQLGELIQ SGPSSSVTSQ SLSRTAERSR
PHRIHSQELQ ESSRGYQPSY NVLPQTFNAV PGLHLVALNA PLKGDMRGIR GADFQCYQQA
RSMGLTTTYR AFLSSHLQDL ATIVRKADRT DMPVVNLRGE VLFSSWMSIF SGNGGTFTPS
TPIYSFDGRN VMTDSAWPEK QVWHGSNTVG IRLTSNYCEA WRTGDMAVTG QAALLQTGRL
LGQHTRSCSN HYIVLCIENT YVGNTHQKRT
//
