ID A0A8I3W5C9_CALJA Unreviewed; 1328 AA.
AC A0A8I3W5C9;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCJAP00000081738.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCJAP00000081738.1};
OS Callithrix jacchus (White-tufted-ear marmoset) (Simia Jacchus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000081738.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000081738.1, ECO:0000313|Proteomes:UP000008225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000081738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000081738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSCJAT00000137838.1; ENSCJAP00000081738.1; ENSCJAG00000083421.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000008225; Chromosome 21.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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:UP000008225};
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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1328
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035251476"
FT DOMAIN 42..230
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 232..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..428
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..524
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..879
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..988
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 134734 MW; 41247B13C3EC8AD2 CRC64;
MAPRWSLLWP RRRRRLLDVL APLVLLLGVR AASAEPESIG EEVGLLQLLG DPLPQQVTQT
EDPDVGLAYV FGPDANSGQV ARYHFPSLFF HDFSLLFHIR PATEGPGVLF AITDSAQAVV
LLGVKLSGVQ DGHQDISLLY TEPGASQTHT AASFRLPTFV GQWTQLALSV AGGSVTLYVD
CEEFQRMPLA RSSRGLELER GAGLFVAQAG GADPDKFQGM IAELKVRGDP QVHCLDEDDD
SDGASGDFGS GLGDAREPLG VETGAALKPR LPTPPPVTAP PLAGGSSMEE SRTEENEEQT
TAPTLGAQTL PGSDSVSTWD GSVRTPGGRM KEGGLKGQKG EPGVPGLPGR AGPPGSPCIP
GPPGPPCPVS PQGPAGPALQ PVPGPQGPPG LPGKDGSPGR DGKPGDPGED GKPGDTGPQG
FPGTPGDMGP KGDKGDPGVG VRGPPGPQGP PGPPGPSFRH DKLTFIDMEG SGFGGDLEAL
RGPRGFPGPP GPPGVPGLPG EPGRFGMNSS DVPGPAGLPG VPGREGPPGI PGLPGPPGPP
GREGPPGRTG QKGSLGEAGA PGLKGSKGDP GPAGARGESG LTGAPGPAGP PGPPGPPGPP
GPGLPAGFDD MEGSGGPFWL TARGADGLQG PPGLPGLKGD PGMPGPPGAK GEVGADGAPG
FPGLPGREGT AGPQGPKGDR GSRGEKGDPG KDGVGQPGLP GPPGPPGPVV YVSEQDGAVR
SVPGSEGRPG FAGFPGPAGP KGDLGSKGER GSPGPKGEKG EPGSIFSPDG SALGPAQKGA
KGEPGFRGPP GPYGRPGYKG EIGFPGRPGR PGMNGLKGEK GEPGDASLGI GMRGMPGPPG
PPGPPGPPGT PLYDSNAFVE LNRPGRPGLP GNRGPAGPKG AKGEVGPPGP PGQFPFDFLQ
LEAEMKGEKG DRGDVGQKGE RGELGGSGPP GPPGPPGYPG IPGPKGESIR GQPGPPGPQG
PPGIGYEGLQ GPPGPPGPPG PPGAPSFPGP HRQTISIPGP PGPPGPPGPP GTMGASSGVR
LWATRQAMLG QVHEVPEGWL IFVAEEEELF VRVRNGFRKV QLEAQTLLTR GLDNEVAALQ
PPVVQLHDSN PHPWRGHPRP TARPWRADDI LASPPRLPEP QPYPGAPHHG SYVHLRPARP
TSPPAHTHLN FQPVLHLVAL NSPLTGSMRG IRGADFQCFQ QARAVGLVGT FRAFLSSRLQ
DLYSIVRRAD RAAVPIVNLK DEVLFPSWEA LFSGSEGLLK TGARIFSFDG KDVLRHPTWP
QKSVWHGSDP SGRRLTESYC ETWRTDAPSV TGQASSLLGG SLLGQNAASC HHAYIVLCIE
NSFMTASK
//
