ID A0A8I3WH65_CALJA Unreviewed; 1319 AA.
AC A0A8I3WH65;
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:ENSCJAP00000088695.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCJAP00000088695.1};
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:ENSCJAP00000088695.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000088695.1, 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:ENSCJAP00000088695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000088695.1}
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; ENSCJAT00000131828.1; ENSCJAP00000088695.1; 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:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 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..1319
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035320220"
FT DOMAIN 42..230
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 232..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1097
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 668..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..870
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 133917 MW; 0E6B8882733E318F 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 DPGMPGPPGA KGEVGADGAP GFPGLPGREG
TAGPQGPKGD RGSRGEKGDP GKDGVGQPGL PGPPGPPGPV VYVSEQDGAV RSVPGSEGRP
GFAGFPGPAG PKGDLGSKGE RGSPGPKGEK GEPGSIFSPD GSALGPAQKG AKGEPGFRGP
PGPYGRPGYK GEIGFPGRPG RPGMNGLKGE KGEPGDASLG IGMRGMPGPP GPPGPPGPPG
TPLYDSNAFV ELNRPGRPGL PGNRGPAGPK GAKGEVGPPG PPGQFPFDFL QLEAEMKGEK
GDRGDVGQKG ERGELGGSGP PGPPGPPGYP GIPGPKGESI RGQPGPPGPQ GPPGIGYEGL
QGPPGPPGPP GPPGAPSFPG PHRQTISIPG PPGPPGPPGP PGTMGASSGV RLWATRQAML
GQVHEVPEGW LIFVAEEEEL FVRVRNGFRK VQLEAQTLLT RGLDNEVAAL QPPVVQLHDS
NPHPWRGHPR PTARPWRADD ILASPPRLPE PQPYPGAPHH GSYVHLRPAR PTSPPAHTHL
NFQPVLHLVA LNSPLTGSMR GIRGADFQCF QQARAVGLVG TFRAFLSSRL QDLYSIVRRA
DRAAVPIVNL KDEVLFPSWE ALFSGSEGLL KTGARIFSFD GKDVLRHPTW PQKSVWHGSD
PSGRRLTESY CETWRTDAPS VTGQASSLLG GSLLGQNAAS CHHAYIVLCI ENSFMTASK
//
