ID A0AAD8GG56_ACIOX Unreviewed; 1367 AA.
AC A0AAD8GG56;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Collagen alpha-1(XV) chain-like isoform X1 {ECO:0000313|EMBL:KAK1173619.1};
GN Name=COL15A1 {ECO:0000313|EMBL:KAK1173619.1};
GN ORFNames=AOXY_G3776 {ECO:0000313|EMBL:KAK1173619.1};
OS Acipenser oxyrinchus oxyrinchus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=40147 {ECO:0000313|EMBL:KAK1173619.1, ECO:0000313|Proteomes:UP001230051};
RN [1] {ECO:0000313|EMBL:KAK1173619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=STURGEONOMICS-FGT-2020 {ECO:0000313|EMBL:KAK1173619.1};
RC TISSUE=Whole blood {ECO:0000313|EMBL:KAK1173619.1};
RA Stock M., Klopp C., Guiguen Y., Cabau C., Parinello H.,
RA Santidrian Yebra-Pimentel E., Kuhl H., Dirks R.P., Guessner J., Wuertz S.,
RA Du K., Schartl M.;
RT "Atlantic sturgeon de novo genome assembly.";
RL Submitted (FEB-2022) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK1173619.1}.
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 EMBL; JAGXEW010000003; KAK1173619.1; -; Genomic_DNA.
DR Proteomes; UP001230051; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; 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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF5; COLLAGEN TYPE XIII ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 4.
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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAK1173619.1};
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:UP001230051};
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..1367
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042056192"
FT DOMAIN 105..293
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 293..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1042
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 141653 MW; 8F0E3315EF191F03 CRC64;
MEQRIFCLYT LLIVVSPVCG QWWWSRFWGT PETTSSPPDI TDTVTTRTKE DVPEDLTGTR
RLSSQLMIQK EVSPVSVKTK YAANKSKNVK RLLKRITFER GSKGLLDLTE LIGVPLPPSV
SFITGFEGFP AYSFGPDANI GRLTKTLITE PFYRDFAVII TIKPTTNQGG VLFAITDAFQ
KVIYLGLALT PVEDDTQRII MYYTEPGSSR SQQVASFKVA GMTNKWNRFT LGVQDNEITL
YMDCEEYHRT TFQRASRPLK FESSSGIFVG NAGGTGLEKF VGSIQQLLIK PDPRAAEEQC
EDDDPYASGA GSGDDTHEEQ DTVDDSKKRV EQVEYNPSLP DEGISRPIQA PPTEAPYSEE
TEDFSGHRPS TILLEQHSED ITFSEERGSS SLRNEQVQSG DRGYGSEAVQ KERVGSGSSG
FEPKGEKGDR GPPGPPGPPG PPRVSTPLPG PAGPVGPPGQ PGPPSKDGET GAAGKDGLPG
ERGPPGFPGL PGDNGIKGEK GDPGVGLPGP PGPPGPPGPS RYPNVLDAYG SGFGDFDSDA
ELVRGPPGPP GPAGQPGPPG PSGPLGASEG HIPGPPGPPG LPGKDGNEGG SGDPGLPVFD
VEFSGSGEGP QGPPGVGGAA GPRGEKGEKG DHGSPGLKGD AGDPGPVGAA GARGSDGQPG
IPGSPGQPGP PGPPGKAFSY GLVDMEGSGE IGAFGKPGPR GPPGAVGKPG PMGPKGENGT
IGLPGIAGEK GNAGLPGKQG QLGVAGLPGQ RGEKGETGDI GQKGEPGQDG KSIIGPPGLP
GPPGQIISLQ DLMFNDTEGI FNFTDIRGPP GPEGMPGRAG FPGPRGPKGA TGFPGVQGPP
GLKGEKGEAG SIIAADGSLM AGLTGPKGPK GIQGEPGLTG PRGPMGPKGP LGPKGEFGFP
GRPGRPGMIG KKGEKGEIVT LPGPPGLPGP PGPPGPAITI KGTVFPVPPR PHCKTPVNGN
KETQHEPTFT HGPKGQKGLF GSKGEKGDNG FSGIPGPKGW WNPDEFKGEK GDSGYKGDKG
EKGEAGVSGP PGLPGRSGLV GPKGESIIGP RGSPGVPGVP GQPGFGRPGP AGPPGPPGPP
SLFGSAVAIP GPPGPPGQPG PSGVGNPTST YRNIEALQKE TYRTAEGTMV YVTDKSEVYI
RVRQGWRKVL LGELIPFPSE IPSLPVASGL EIQSFLPGYN LLPHTVHTQP GLHLVALNAP
FSGDMRGIRG ADFQCFQQAR AMGLMATYRA FLSSHLQDLA TIVKKGDRFN MPIVNLKGEV
LFNNWMSIFS GNGGQFDHQI PIYSFDGRNV MSDPSWPQKM IWHGSNRNGI RQTSNYCEAW
RAGDMAVTGQ ASLLQSGRLL DQHTRSCSNN FIVLCVENSY VHDHRRK
//
