ID A0A1S3GJE8_DIPOR Unreviewed; 1417 AA.
AC A0A1S3GJE8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_012888354.1};
GN Name=Col18a1 {ECO:0000313|RefSeq:XP_012888354.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888354.1};
RN [1] {ECO:0000313|RefSeq:XP_012888354.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888354.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_012888354.1; XM_013032900.1.
DR FunCoup; A0A1S3GJE8; 169.
DR STRING; 10020.ENSDORP00000010789; -.
DR GeneID; 105998234; -.
DR KEGG; dord:105998234; -.
DR CTD; 80781; -.
DR InParanoid; A0A1S3GJE8; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000081671; Unplaced.
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 FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1107; COLLAGEN TYPE XXVI ALPHA 1 CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_012888354.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000081671};
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..1417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010338956"
FT DOMAIN 326..445
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 53..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..919
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 341..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1417 AA; 144062 MW; AE027B9207583C4E CRC64;
MAPDPSGRLC LLLPTPLLLL LLLLLPCLPS AGANLLSLEW LWSSKLSDSP ATLVPRPTHA
GPRHDPTEPA PLSASPELPR EHQGPGRPGP SAPPTAPATP AASPDTKEEN IAGVGAKILN
VAEGIRSFVQ LWDDATPTPN SAVADPPTHT GLSSNPQESR TILWPSSGAL GSPDTQSPEA
STLAAPTQPS PSWSRTQAPQ WGSTAPPVPT GRAPLSSIPG RAPAWQPGHL DRGRRLPVAA
GPSPRHGCPE GPVAPMLTPL LLPLVVGPLA TRSASSAPPS APSARLAQVA APAPCGDRGA
WFSHGAGSPV PGLANNAALL GAAPQAPAGR CLPLPPGLPV CSHLGFGHSW LPNLLHHKSS
EEVRAAARAW TGLLRTHCHP FLAWFFCLLL APPCGPGPGP PPALPPCRQF CKVLEDACWS
GLEGAGLPIP CASLPDQEEG YCVFIGPAAE SAVEEVGLLQ LLREPLPPQI TPIEDPDVGP
AYDFGPGANS GQGAQSHFPR LFFRDFSLLF HIRPATAGPG VLLAITDAAQ ALVSLGVKLS
EVQGGYQNVS LLYTEPGAAQ THVAASFRLP ALVGRWTRFA LSVDGGTVAL YLDCDEFQRV
PFARSLPGLE LEHGAGLFLG QAGGADADKF QGAIAELRVR GDPKVNLGHC LDEEDDDEDG
ASGDFGSGLE DGHRPHGEDT DTPLQPGLPL PSPASLPPLA GGSPMESSRT EETEDEIMVD
SFGAPTLPDS ESAGVWDRGV QSPEGGLETG VLSRQKEESG VPGPGLVVQG SDLQHVPVAQ
GPPGPPGPPG KDGSPGQDGK PGDPGEDGKP GDAGPQGFPG TPGDVGPKGE KGDPGVGPRG
PPGPQGPPGP PGPPFRQDKL TFIDMEGSGF SGDLEPLRGP RGFPGPPGPP GVPGLPGEPG
HFGVNSSHVP GPAGLPGVPG RDGRPGPPGV QGDPGKDGVG QPGLPGPPGP PGPVVYVSDQ
DGQPAVAGVA GPEGRTGHGG LRGPTGPKGD LGSKGEQGLP GPKGEKGEPG GFYGADGRAL
GPAQKGAKGE PGFRGPPGPY GRPGHKGEIG IPGRPGRPGV NGLKGEKGEP GDTSLGLGMR
GMPGPPGPPG PPGPPGVPVY DSNAFMEAGR PGPKGLQGAQ GPSGPKGDKG EVGPPGPPGQ
FPLDLLHLEA EMKGEKGDRG DAGQKGERGE PGPSGGFFGS SVPGPPGPPG PPGYPGIPGP
KGESIRGQPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV PGPPGPPGPP
GPPGAMGASS GVRIWATYRT MLDRVREVPE GWLIFVTERE ELYVRVRNGF RKVLLGAQTS
LPPASVSGVF PLHHRQCLRV LIPGRARPQK SVWHGSDPNG RRLTESYCET WRTEASSAAG
QASSLLAGRL LEQKAAGCHN PYVVLCIENS FMTSASK
//
