ID A0A6J2VX00_CHACN Unreviewed; 1736 AA.
AC A0A6J2VX00;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_030637590.1};
GN Name=col18a1b {ECO:0000313|RefSeq:XP_030637590.1};
OS Chanos chanos (Milkfish) (Mugil chanos).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gonorynchiformes;
OC Chanidae; Chanos.
OX NCBI_TaxID=29144 {ECO:0000313|Proteomes:UP000504632, ECO:0000313|RefSeq:XP_030637590.1};
RN [1] {ECO:0000313|RefSeq:XP_030637590.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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}.
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_030637590.1; XM_030781730.1.
DR GeneID; 115818370; -.
DR CTD; 100334893; -.
DR InParanoid; A0A6J2VX00; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000504632; Chromosome 8.
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: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; 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; 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 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 Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_030637590.1};
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 Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000504632};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1736
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026932709"
FT DOMAIN 186..303
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 66..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..83
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..120
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..608
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..629
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..982
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1096
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1115
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1213
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1379
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 201..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1736 AA; 180196 MW; 388C95E2D80EF181 CRC64;
MSFWSGLTLL LAFCLVPLDA WFWNSKPAAT EPPTAQNGSE DKNLAGVGAE IIDVASGIRK
FVETWDQDPT TGDTKLTTEK TSTVSQKQGR TKTGNDRSLL GEAEAQSGRE GSSGYASSSG
PGLGSEVTVA STIQSGKEGR EKPVSTNSSK HHGKPFNTSM PSWNATNTDL RPEEGTLTSP
ENGTSTAPPN CVPRGSDWPF CTARGTAGFA APNFLNHSRA EEVGAVLRDW AWLLRSGCHH
GVEWFFCLLL APGCGRSAAL LPCRSFCEVL LDSCWVLLQE GGLPVPCHTL PEGPDHDLPC
VSVSNHKEES GVSLFQLIGS PPPSGVKQID GPDNNPAFLF SEKANAGQLA RTHLPSPFYR
DFSLLFHLQP TSTDAGVIFS ITDADQKVMY VGVKLSAVEA GSRKVIFYYT EPGEKISKEV
ASFKVPHDPE NWSRFSLAIN MNQVSFYGEC DSEPKVVTFE RSPDDVELET GAGIFVGHGG
AADPDKFKGA ISELKLVGNP RAAERHCDED DDDSDYGSGE DYGSGVEGTD SYSEKKIPSV
LQPLPPPPVS SGPSKAYLDT DERQLGGTGA KGEKGDRGEK GDQGDRGLAG PKGDSGPSVS
SGSSIVAGGE KGEQGEKGMK GGPGAGYPGA KGEPGPPGPP GPPGPQGPAA ELVKVGDGTV
VQRVEGKMGP RGLPGPPGPP GPPGPEGDPG DPGEEGKVGP VGPQGHPGLP GTPGSKGQKG
DKGEGQPGPR GPPGLPGPPG PPFSDKPTFV DMEGSGYDRV VGVPGPPGPP GPPGPPGPMI
PGGTGSATAG FGPQGPPGQD GTPGKPGPPG RPGLPGTPGP PGPPGEKGDC GELGLPGAVG
VQGTQGSPGD PGRPGEVGLA GLPGPMGPVG PPGPPGPPGP PGVSYERKDD GTEIAISYIP
GVEGPTGPRG PQGIPGLPGK PGIPGTPGEK GSEGPRGRDG IPGMDGFPGK WGEKGERGSK
GERGLPGREG GPPGPPGPPG PPGQIIYSTS SSFEGVQGAR ESQFGPGVPG LAGFPGPMGP
KGERGQPGPP GDSIKGQKGE PGLILGQDGQ PLYLGGLAGQ PGERGPEGPE GPPGPIGPPG
MKGEIGLPGR PGRPGLNGVK GEKGDSGVGP GGYGYPGPPG PPGPPGPPGP PTPVDRYRYD
DNSRFYIATK GDKGERGTPG IPGLPGLTTN FDIYSFKNEM KGERGDPGMK GEKGEPGGGY
YDPRYGGGQG QPGISGPQGP KGDSVIGPPG QPGPPGPPGI GYDGRPGLPG PPGPPGPPGP
PYRTSQPISI PGPPGPPGPP GRSGLGSGVV VLRSYDAMAA TTRRQPEGTL VYVVDNTDFY
VRVRDGVRQV MLGEYTPFPR EPVNEVAAVD PPSVVEYSPD YTATAPPRTA PQPVDQQPVL
PDPGYPSPYD PRYASPPDPR YPSHTDPQYP PSTDTRYSGQ TDPRYSGPAD PRYSSPTDPR
YPPPTDPRYS GQTDPRYSSP TDPRYSSPTD PRYSSPTDPR YSSPTDPRYS SPTDPRYSSP
TDPRYTSPTD PRYSSPTDPR YHAHQPDSRY PGSQYPHSHY PSTTQRKPSP PVSQRPVHNH
ASGSALHLIA LNAPQAGNMR GIRGADHQCF VQAQAAGFKG TFRAFLSSRL QDLHSIVRRS
DRHNIPIVNL KDEELFSSWE SMFDGSEGKK RENVAIYSFD GKDVLRDDTW PEKMVWHGSN
SQGQRQTDSY CETWRVGDRA VTGMASSLQD GHLLQQAPRS CSSSYILLCI ENSYIP
//
