ID A0A8B8X8F7_BALMU Unreviewed; 1517 AA.
AC A0A8B8X8F7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X6 {ECO:0000313|RefSeq:XP_036705933.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_036705933.1};
OS Balaenoptera musculus (Blue whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036705933.1};
RN [1] {ECO:0000313|RefSeq:XP_036705933.1}
RP IDENTIFICATION.
RC TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036705933.1};
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_036705933.1; XM_036850038.1.
DR GeneID; 118894177; -.
DR CTD; 80781; -.
DR Proteomes; UP000694857; Chromosome 4.
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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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_036705933.1};
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:UP000694857};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034562121"
FT DOMAIN 228..417
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 278..416
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 40..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..107
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..558
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..703
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..764
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..937
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1030
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 153598 MW; E92E31A3971DF581 CRC64;
MAPDPSGRRG HCGLLLLLAC CLAPARADLM SWLWPGNAAG STVAPASTPP GSSPVRPTED
TTTHVAPQDD PTQQWKALAS PEPPLERPEV GQGQAPAVPS AVSTASPDTK EENIAGVGAK
ILNVALGIRS FVQLWDDTTP TESSATAGTP GPGNPTDPLT TPGPSSGPQD GGTTVWLSTG
APSSPDAQRT EAGTLPAPTQ PPPSPDRPRA LLREPAVPPP SPDSQVMEVG LQLLLGEPLP
RQVALVHDPD VGPAYEFGVD VGGDGWAARS LLPSTFFRRF SLLVRVRPAS ARAGVLFAVT
DAAQAVVLVG VKLAAARGAW QQVQLLYTEP GAARTHTAAS FALPALDGRW TRLALTVDGT
HAALFVDCKE VQRQPLARSP RGLQLEPDAR LFVAQAGRAD PDKFQGLISD LRLREEPQVS
PLHCLDEDEE DDDDRASGDL GSGLAETWEH IGEELGAPLG PRLPEAPPVT SPPLAGVGNQ
EDFRTEETEE ETTVSSLGAQ TLPSLSTVTT WAGSEWSPGR GLKEGGLKGQ KGEPGAQGPP
GPVGPQGPAG PAVQSPDAQP VPGPQGPPGP PGKDGAPGRD GEPGDPGEDG KPGDTGPQGF
PGTPGDVGPK GEKGDPGVGP RGPPGPQGPP GPPGPSFRHD RLTFIDMEGS GFGGDLESLR
GPRGVPGPPG PPGVPGLPGE PGRFGMNSSD VPGPAGLPGV PGRDGPPGLP GPPGPPGPPG
KDGRPGQTGQ KGSLGEAGAP GPKGSKGDPG PIGTPGEHGL AGHPGPAGPA GPPGPPGPPG
PPGPGLAAGF DDMEGSGGPF WSTARGASGP QGPLGPPGVK GDPGVMGPPG TKGEVGADGA
PGAPGLPGRE GAAGLQGPKG EKGPQGEKGD PGKDGVGQPG LPGPPGPPGP VVYVSEQDRA
LASVPGPEGR AGLAGLPGPA GPKGDLGSRG QQGLPGPKGE KGEPGMVFSP DGRALTSAQK
GAKGEPGFRG PPGPYGRPGH KGEIGFPGRP GRPGMNGLKG EKGEPGDASV GFSARGPPGP
PGPPGPPGLP GTPVYDSNAF VESGRPGPPG LPGNQGPSGP KGDKGEVGPP GPPGQFPFDL
LHLGAEMKGE KGDQGAAGQK GERGEPGGGG FFSSSMPGPP GPPGYPGIPG PKGESIQGQP
GPPGPQGPPG IGYEGHQGPP GPPGPPGPPG PPSFPGPYRQ TISVPGPPGP PGPPGPPGSM
GTSSGQVRVW ATYQTLLDQV PEVPEGWLVY VADREELYVR VRNGFRKVLL EARTPLPRGT
DNEVAALQPP VVQLHEGNPY PRREPPPPTA RSWRADDILA GPPRLTHAQP YPRAPHPGAY
AHLRPATPTA SPAHTHHDFQ PVLHLVALNS PQSGGLRGIR GADFQCFQQA RAAGLAGTFR
AFLSSRLQDL YSIVRRADRA ALPIVNLRDE VLSPSWEALF SGSEGQLKPG ARIFSFDGRD
VLQHPAWPQK SLWHGSDPSG RRLTESYCET WRTEARAATG QASSLLAGRL LEQKAAGCYN
AFIVLCIENS FMTSSSK
//
