ID A0AAD9BJF7_DISEL Unreviewed; 1022 AA.
AC A0AAD9BJF7;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE SubName: Full=Collagen alpha-4(VI) chain {ECO:0000313|EMBL:KAK1884995.1};
GN ORFNames=KUDE01_031191 {ECO:0000313|EMBL:KAK1884995.1};
OS Dissostichus eleginoides (Patagonian toothfish) (Dissostichus amissus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=100907 {ECO:0000313|EMBL:KAK1884995.1, ECO:0000313|Proteomes:UP001228049};
RN [1] {ECO:0000313|EMBL:KAK1884995.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE {ECO:0000313|EMBL:KAK1884995.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1884995.1};
RA Park H.;
RT "Chromosome-level genome of Chaenocephalus aceratus.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
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:KAK1884995.1}.
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DR EMBL; JASDAP010000021; KAK1884995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD9BJF7; -.
DR Proteomes; UP001228049; Unassembled WGS sequence.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAK1884995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001228049}.
FT DOMAIN 845..892
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 924..1008
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 74..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..168
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..211
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..772
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 105048 MW; B6A4C734E4B0A449 CRC64;
MGDMTGRWAR FSLTVQGAEV RLYMDCEEYH RVAFSRSPQP LTFEPSSGMF IGNAGGTGLQ
RFVGSIQQLV LKSDPTAPDD QCEEDDPYAS GYGSGDDAYD DFEGRDEVKK IVNTMPLPEL
DPSYSAPVQA PPTEMSRGFV DDEDIEEISG QEVEKTTVTV KSSPTVTPAS IRDTSLQVSS
GQKGEQGEPG PSGPPGPPGT ASGGGEGGEP GPRGPQGPAG SSGKPGASGK DGQAGSKGET
GDQGATGVPG FPGLQGDSGP IGEKGDPGLG HPGPPGPPGP PGPTSKSSMF LEGSGGLEDF
DSDAEILRGP PGPPGVPGQP GPPGAQSENM FPGSPGAPGK DGKDGQRGEP GVPGVDGKDG
DPGSAGENGD KGEPGVNGQP GTKGDQGPAG FPGQPGSEGP EGHPGPRGAP GPPGPPGKGY
SMDFEDLEGS GMQGGFGSAL SRGPEGPAGV PGIQGPMGKD GLDGAAGKPG ERGEKGATGS
PGFPGLDGFK GEEGLKGDKG DPGQKGEVGR DGLSIPGPPG PPGPPGPLIN LQDLQLNDTD
GTFNFSGIFE AQGPAGPQGP KGDGGLPGVQ GPSGIKPTDR CRRAWLLHQE SRVIMVYLDL
LEFKARPDLQ DQRESLVFLE DLVVRAGWGL KEREGTLQAC RDFRALQGCR AAQVYSTAPK
EPHCKQTRGA RMALNLSCML HVHSGKVKAQ CKYIQELNPD GTVAVGNCQT GWKGERGERG
LPGLPAPQSS FLSRGGWGSS GDQGLKGEKG ERGEEGFSGT PGTPGRSGPV GPKGESVIGP
QGPPGVPGSP GFPGYGRPGP VGPAGPPGPP GPSGTPLRYG SALTIAGPPG PPGPSGPSGS
SSSMKTFTSR ESMMQHTVRD AEGTMAYVTS TGSLFIKVSQ GWKEIQLGSL IYLSNNIIPQ
DEPRIAYQIR GETMERIRSV NERLTLVALN QPHSGHMTGL DTADRLCYEQ AKAMGLAPNY
RAFISSNRQD LVHVVYPGFR ENLPVTNLRG DVMFRNWREI FTGDGGRWMP EYPSTPSTVG
TL
//
