ID A0A1U8BQ55_MESAU Unreviewed; 1322 AA.
AC A0A1U8BQ55;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X5 {ECO:0000313|RefSeq:XP_012969357.1};
GN Name=Col18a1 {ECO:0000313|RefSeq:XP_012969357.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012969357.1};
RN [1] {ECO:0000313|RefSeq:XP_012969357.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_012969357.1; XM_013113903.2.
DR GeneID; 101836799; -.
DR CTD; 80781; -.
DR OrthoDB; 5363002at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 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; 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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00210; TSPN; 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,
KW ECO:0000313|RefSeq:XP_012969357.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1322
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010583131"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 227..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 135116 MW; 833E798F9186E377 CRC64;
MEPRWHRLRR RHLLDVLTSL VLLLVVRVAW AKPENVAEEV GLPQLLGDPL PQQITQIDDP
HVGPVYIFGR DSSSSQTAQH HFPRLFFRDF SLLFHIQPAT KAAGVLFAIT DTVQKVVSLG
VKLSGVQNGH QNISLLYTEP GATQTQTGAS FHLPAFVGQW THFVLSVDGG SVTLYVDCEE
FQRVPFARSP QGLELEHGSG LFVGQAGAAD PDKFQGKISE LKVRQNPRVS PVLCSDEDGD
DEDRASGDFG SGFEESSKPH REEDTSLAPS LPQPPPVTSP PLAGGSTTED SRTEETEEET
TVDSIGAETL PGTDSSRARD ESVQNHGGGL IKGGLKGQKG EPGARGLPGP AGPQGPAGPV
IQSPIAQPVP GAQGPPGPQG PPGKDGAPGR DGEPGDPGED GRPGDAGPQG FPGTPGDVGP
KGEKGDPGVG ARGPPGPPGP PGPSFRQDKL TFIDMEGSGF SGDLESLRGP RGFPGPPGPP
GVPGLPGEPG RFGVNSSYAP GPAGLPGVPG KEGPPGFPGP PGPPGPPGKV GPPGEAGQKG
NVGEVGIPGP KGSKGDLGPV GVPGKTGMAG PPGPTGPPGP PGPPGPPGPG FAAGFDDMEG
SGIPFWSTAR SSEGLQGPPG LPGLKGDPGV TGPPGAKGEV GAEGVQGMPG LPGRAGAAGS
PGPKGEKGSQ GEKGSPGKDG VGLPGLPGPP GPPGPVLYVS NEDRAVVTTP GPEGKPGYAG
FPGPAGPKGD LGSKGEQGLP GPKGEKGEPG AIFGPDGRAL GHAQKGAKGE PGFRGPPGPY
GRPGHKGEIG FPGRPGRPGT NGLKGEKGEP GDASLGFSMR GLPGPPGPPG PPGPPGMPIY
DSNAFVESGR PGLPGQQGVQ GPSGPKGDKG EVGPPGPPGQ FPIDFFNLGA EMKGDKGDRG
DTGQKGERGE PGVAGGGFFS SSVPGPPGPP GYPGIPGPKG ESIRGPPGPP GPQGPPGIGY
EGRQGPPGPP GPPGPPSFPG PHRQTVSVPG PPGPPGPPGP PGAMGASAGQ VRIWATYQTM
LDKVREVPEG WLIFVAEREE LYVRVRNGFR KVLLEARTAL PHGTGNEVAA LQPPLVQLHE
GSPYTRREHS YSTARPWRAD DILANPPRLP EPQPYPGVPH HHSSSVHQPP AHPTGSPAHT
HHDFQPVLHL VALNSPLSGG MRGIRGADFQ CFQQARAVGL AGTFRAFLSS RLQDLYSIVR
RADRGTVPIV NLKDEVLSPS WDALFSGSQG QLQPGARIFS FDGRDVLRHP VWPQKSIWHG
SDPSGRRLME SYCETWRTEA TGATGQASSL LSGRLLEQKA ASCHNTYIVL CIENSFMTSF
SK
//
