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Database: UniProt
Entry: A0A6J1XY86_ACIJB
LinkDB: A0A6J1XY86_ACIJB
Original site: A0A6J1XY86_ACIJB 
ID   A0A6J1XY86_ACIJB        Unreviewed;      1306 AA.
AC   A0A6J1XY86;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 2.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Collagen alpha-1(XVIII) chain isoform X5 {ECO:0000313|RefSeq:XP_026897210.2};
GN   Name=COL18A1 {ECO:0000313|RefSeq:XP_026897210.2};
OS   Acinonyx jubatus (Cheetah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae;
OC   Acinonyx.
OX   NCBI_TaxID=32536 {ECO:0000313|Proteomes:UP001652583, ECO:0000313|RefSeq:XP_026897210.2};
RN   [1] {ECO:0000313|RefSeq:XP_026897210.2}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_026897210.2};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_026897210.2; XM_027041409.2.
DR   GeneID; 106985669; -.
DR   Proteomes; UP001652583; Chromosome C2.
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:0032836; P:glomerular basement membrane development; IEA:TreeGrafter.
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; 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: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; 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   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119,
KW   ECO:0000313|RefSeq:XP_026897210.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP001652583};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1306
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5046570310"
FT   DOMAIN          41..229
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          232..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..345
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..361
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..425
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..499
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..519
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..554
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..571
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..677
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..819
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..847
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..892
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..916
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..962
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..984
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1306 AA;  132607 MW;  079817500E902391 CRC64;
     MAPRWPWLRP RPRSLLDVLA PLVLLLGVRA ASADPESLGT EVGLLQLLGE PPPQQVAQVD
     DPDVGPAFVF GPDANSGQVA RYHFPSPFFR DFSLLFHVRP ATEGAGVLFA ITDAAQAVVS
     VGVKLSAVRD GQQHIQLLYT EPGATRTHTA ASFRLPAFTG QWTRFALSVD GATVALFVDC
     ELFQRVPLVR SPRALELEPG AGLFVAQAGG ADPSKFQGRI AELRVRGDPR VSPLHCLEED
     DEDSGGVSGD FGSGLEENRE LLREQSRLSP KPSLPEAPPV TSPPLAGGRN VEDSRTEEIE
     EETTMSSLGA WTLPGSDTVT AWSVRSPGGG PEEGPAGSAV QSPDAQPVPG PQGPPGPPGP
     PGKDGAPGKD GEPGDPGEDG KPGDPGPQGF PGTPGDMGPK GEKGDPGVGP RGPPGPQGPP
     GPPGPSFRHD RLTFIDMEGS GFGGDLESLR GPRGFPGPPG PPGVPGLPGE PGRFGMNSSD
     VPGPAGLPGV PGRDGAPGLP GAPGPPGPPG RDGGPGKTGQ KGSPGEAGAP GPKGSKGDPG
     PTGAPGETGL AGAPGPAGPP GPPGPPGPPG PGLAAGFEDM DGSGGPFWST AHGASGPQGP
     PGLPGVKGDP GIAGPPGAKG EVGADGPPGF PGLPGREGTA GAQGPKGEKG TQGEKGDPGR
     DGVGQPGLPG PPGPPGPVVY VSEQDRAVAG VPGPEGRPGY AGFPGPAGPK GDLGSKGQRG
     PPGPKGEKGE PGPVFSPDGG TLGPAQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP
     GMNGLKGEKG EPGHASVGFG VRGPPGPPGP PGPPGPPGTP VYDSNDFMES GRPGPPGLPG
     YQGPPGPKGD KGEVGPPGPP GQFPLDLLQL EAEMKGEKGD RGDPGQKGER GEPGGGGFFG
     SSVPGPPGPP GYPGIPGPKG ESIRGQPGPP GPQGPPGIGH EGRQGPPGPP GPPGPPGPPS
     FPGPYRQTIS VPGPPGPPGP PGPPGTMGTS SGQVRIWATY QTMLDKVPEV PEGWLIFVAE
     TEELYVRVRN GFRKVLLEAR TPLPRGTDNE VAALQPPLVQ LHEGNPYPRR ELTHSTARPW
     RADDILAGPP RLPDPRPYPG APHHGPYLHV QPARPTGGPA RTHTHQDFQP VLHLVALNSP
     QPGGMRGIRG ADFQCFQQAR AVGLAGTFRA FLSSRLQDLY SIVRRADRTG VPIVNLRDEV
     LFPSWEALFS GSEGQLKPGA RVFSFDGRDV LQHPAWPQKS VWHGSDPSGR RLTDSYCETW
     RTEDAAAAGQ ASSLLAGRLL AQKAASCRNA FIVLCIENSF MTSSSK
//
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