ID A0A2K6A7P3_MANLE Unreviewed; 1728 AA.
AC A0A2K6A7P3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSMLEP00000036043.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000036043.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000036043.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMLEP00000036043.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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_011857984.1; XM_012002594.1.
DR STRING; 9568.ENSMLEP00000036043; -.
DR Ensembl; ENSMLET00000059643.1; ENSMLEP00000036043.1; ENSMLEG00000042137.1.
DR GeneID; 105555574; -.
DR KEGG; mleu:105555574; -.
DR CTD; 80781; -.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000233140; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
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 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; IPR035523; Collagen_XVIII_Fz.
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:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 1.
DR Pfam; PF01391; Collagen; 4.
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 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1728
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014457510"
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 655..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1529
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 688..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..817
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..913
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1038
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1127
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1525
FT /note="Pro residues"
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 1728 AA; 175442 MW; BEB528B55A9D75B2 CRC64;
MAPDPSGCRV LLLLFCCLAA AQADLLNLNW LWFNNKDTSQ AATTIPEPQG LLPVQPTADT
TTHVVPQDGS TEPATAPGSP EPPSELLEDS QVTPTSAESP DTPEENIAGV GAKILNVAQG
IRSFVQLWND TVPTESLARA ETRVVEAPVG TLALPGPSST PRENGTSLWP SRGAPSSPGA
HMTEAGTLPA PTPSPPSLGR PRAPLTGPSV PPPSSGRASL SSSLGGAPAW GSLQDPDSRG
LSPTAAAPSQ QLQRPDVSLR TPLLHPLVTG SLGAHAAPSA FSSGLPGALS QVAVTTLIGD
SGAWVSHAAN SAGLGLANNS ALLGADPEAP AGRCLPLPPS LLVCGRLGIL RSWLPNHLHH
ESSQQVQAAA QVWGGLLRTH CHPFLAWFFC LLLAPPCGRV PLPAPPPCRQ FCEALQDTCW
SRLSGGRLPV ACASLPTQED GYCVFIGPAA ESVGEEVGLL QLLGDPPPQQ ITQTDDPDVG
LAYVFGPEAN SGQVARYHFP SLFFRDFSLL FHIQPATEGP GVLFAITDSA QAVVSLGVKL
SGVRDGHQDI SLLYTEPGAG QTHTAASFRL PAFVSQWTHL ALSVEGGYVA LYVDCEEFQR
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQASGDFGSG LADTRELLRE EMGTALKPRL
PTPPPVTAPP LAGGSSTEDS RSEEIEEQTT VTSLGAQTLP GSDSVSTWDG SVQTPGGRVK
EGGLKGQKGE PGIPGPPGRA GPPGSPCLPG PPGLPCPVSP LGPVGPALQP VPGPQGPPGL
PGRDGTPGRD GEPGDPGEDG KPGDTGPQGF PGTPGDVGPK GDKGDPGVGA RGPPGPQGPP
GPPGPSFRHD KLTFIDMEGS GFGGDLEALR GPRGFPGPPG PPGVPGLPGE PGRFGVNSSD
VPGPAGLPGV PGREGPPGFP GLPGPPGPPG KEGPPGRTGQ KGSLGEAGAP GHKGSKGDAG
PAGARGESGL AGAPGPAGPP GPPGPPGPPG PPGRGLPAGF DDMEGSGGPF WSTARGADGP
QGPPGLPGLK GDPGVPGLRG AKGEVGANGA PGFPGLPGRE GTAGPQGPKG DRGSQGEKGD
PGKDGVGQPG LPGPPGPPGP VVYVSEQDGA VLSVPGPEGR PGFAGFPGPA GPKGDLGSKG
ERGSPGPKGE KGEPGSVFSP DGSALGPAQK GAKGEPGFRG PPGPYGRPGH KGEIGFPGRP
GRPGMNGLKG EKGEPGDAHL GFGMRGMPGP PGPPGPPGPP GTPVYDSNVF AESSRPGPPG
LPGNQGPPGP KGTKGEVGPP GPPGQFPFDF LQLEAEMKGE KGDRGDAGQK GERGEPGGGG
FFGSSLPGPP GPPGPPGYPG IPGPKGESIR GQPGPPGPQG PPGIGYEGRQ GPPGPPGPPG
PPGPPSFPGP HRQTISVPGP PGPPGPPGPP GTMGTSSGVR LWATRQAMLG QVHEVPEGWL
IFVAEQEELY VRVRNGFRKV QLEPRTPLPR GTDNEVAALQ PPVVQLHDSN AYPRREFPHP
TARPWRADDI LASPPRLPEP QPYPGAPHHS SYVHLRPALP TSPPAHTHRD FQPVLHLVAL
NSPLPGGMRG IRGADFQCFQ QARAVGLVGT FRAFLSSRLQ DLYSIVRRAD RAAVPIVNLK
DELLFPSWEA LFAGSEGPLK PGARIFSFDG KDVLRHPTWP QKSVWHGSDP SGRRLTESYC
ETWRTESPSV TGQASSLLGG RLLGQNAASC HHAYIVLCIE NSFMTASK
//
