ID A0A2K5MXS9_CERAT Unreviewed; 1553 AA.
AC A0A2K5MXS9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCATP00000030053.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCATP00000030053.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030053.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000030053.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCATP00000030053.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 9531.ENSCATP00000030053; -.
DR Ensembl; ENSCATT00000054314.1; ENSCATP00000030053.1; ENSCATG00000038222.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000233060; Unassembled WGS sequence.
DR Bgee; ENSCATG00000038222; Expressed in liver and 10 other cell types or tissues.
DR GO; GO:0005594; C:collagen type IX trimer; 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 CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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 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; IPR035523; Collagen_XVIII_Fz.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
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:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 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; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014439598"
FT DOMAIN 329..446
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 47..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..747
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..841
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..886
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1156
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 344..390
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 381..419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1553 AA; 159356 MW; 7C57518CC80BB6FF CRC64;
MAPDPSGCRV LLLLFCCLAA AQADLLNLNW LWFNNKDTSQ AATTIPEPQG LLPVQPTADT
TTHVVPQDGS TEPATAPGSP EPPSELLEDS QGTPTSAESP DTPEENIAGV GAKILNVAQG
IRSFVQLWND TVPTESLARA ETRVVEAPVG TLALPGPSST PRENGTTLWP SRGAPSSPGA
HTTEAGTLPA PTPSPPSLGR PRAPLTGPSV PPPSSGRASL SSSLGGAAAW GSLQDPDSRG
LSPTAAAPSQ QLQRPDVRLR TPLLHALVTG SLGVHAAPSA FSSGLPGALS QVAVTTLIGD
SGAWVSHAAN SAGLGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS RSWLPNHLHH
ESSQQVQAAA QVWGGLLRTH CHPFLAWFFC LLLAPPCGRV PLPAPPPCRQ FCEALQDTCW
SRLSGGRLPV ACASLPTQED GYCVFIGPAA ESVSEEVGLL QLLGDPPPQQ ITQTDDPDVG
LAYVFGPEAN SGQVARYHFP SLFFRDFSLL FHIQPATEGP GVLFAITRQW SRWGMIAELK
VRRDPQVGPM HCLDEEGDDS DGASGDFGSG LADTRELLRE EMGTALKPRL PTPPPVTAPP
LAGGSSTEDS RSEEIEEQTT VTSLGTQTLP GSDSVSTWDG SVRTPGGHVK EGGLKGQKGE
PGIPGPPGRA GPPGSPCLPG PPGLPCPVSP LGPVGPALQP VPGPQGPPGL PGRDGTPGRD
GEPGDPGEDG KPGDTGPQGF PGTPGDVGPK GDKGDPGVGA RGPPGPQGPP GPPGPSFRHD
KLTFIDMEGS GFGGDLEALR GPRGFPGPPG PPGVPGLPGE PGRFGVNSSD VPGPAGLPGV
PGREGPPGFP GLPVSPASGV LSAGSGGKGD PGPAGARGES GLAGAPGPTG PPGPPGPPGP
PGRGLPAGFD DMEGSGGPFW STARDSSWGS PHSWGEVGAN GAPGFPGLPG REGTAGPQGP
KGDRGSQGEK VSVPGADGWG EGALGHLEGL ASGAVLSVPG PEVRACPGPA GPKGDLGSKG
ERGSPGPKGE KGEPGSVFSP DGSALGPAQK GAKVRGPYGR PGHKGEIGFP GRPGRPGMNG
LKGEKGEPGD AHLGFGMRGM PGPPGPPGPP GPPGTPVYDS NVSPQGAHCP AAALGSYTEP
HRGAGPSSLA SASAGPSGMG QFPFDFLQLE AEMKVGDLPG GVEGPQGPVH PPGWLLPIPC
AIRPKTPSCS ALRGHPETGI PSFCPCPVPS HLEPHAPAFG SQQVRLWATR QAMLGQVHEV
PEGWLIFVAE QEELYVRVRN GFRKVQLEPR TPLPRGTDNE VAALQPPVVQ LHDSNPYPRR
EFPHPTARPW RADDILASPP RLPEPQPYPG APHHSSYVHL RPALPTSPPA HTHRDFQPVL
HLVALNSPLP GGMRGIRGAD FQCFQQARAV GLVGTFRAFL SSRLQDLYSI VRRADRAAVP
IVNLKDELLF PSWEALFAGS EGPLKPGARI FSFDGKDVLK HPTWPQKSVW HGSDPSGRRL
TESYCETWRT ESPSVTGQAS SLLGGRLLGQ NAASCHHAYI VLCIENSFMT ASK
//
