ID A0A6P7H325_9TELE Unreviewed; 1534 AA.
AC A0A6P7H325;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen type XVIII alpha 1 chain a isoform X1 {ECO:0000313|RefSeq:XP_028249445.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_028249445.1};
OS Parambassis ranga (Indian glassy fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Ambassidae; Parambassis.
OX NCBI_TaxID=210632 {ECO:0000313|Proteomes:UP000515145, ECO:0000313|RefSeq:XP_028249445.1};
RN [1] {ECO:0000313|RefSeq:XP_028249445.1}
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_028249445.1; XM_028393644.1.
DR GeneID; 114426317; -.
DR CTD; 564123; -.
DR InParanoid; A0A6P7H325; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000515145; Chromosome 21.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
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_028249445.1};
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:UP000515145};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 82..200
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 399..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..487
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..579
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..715
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..773
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..840
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1039
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 97..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1534 AA; 158672 MW; C2CF4FA19E5CFD24 CRC64;
MSITQIADTT LISMTNQPHI PRQTLITSQK EVTSQTAHIL GATQPSVSKQ ELSIETSFSQ
TAEGSQATTE AHTEVVKSAL DVESPQCLLL DTPLPFCSFV VGEKFVVPNY FNHSSVEEVH
ALLKEWEWLL RSSCHHSLEW FFCLLLVPKC QQQVVLPCQS FCQVLRDSCW TLLDEGRLPV
ECHTLPDEKD DDDGYQCLSV CNQKEDSGVS LLQLIGDPPP NEITRVYGTD NNPAYVFGPD
ANTGQLARAH FPSPFYRDFA LIFNLKPTSD RGGIIFSITD ASQQIMYVGV KLSEVQGSNQ
NLILYYTEPD SQQSYEAARF LVPSMRDVWT RFAIAVRDDK VMFYLNCDAD PQVMRIERSP
DEMELEGGAG VFVGQAGGAD PAKFLGVIGE LRVVGDPRAA ERHCEEDGDD SDMASGEGSG
YEETRPPKPG AEKHKSTTMP PSSRPIQQPP LKNEVAMARE TASDSQHLSV SVESRPGLPG
SPGAAGAKGE KGDKGDRGEK GDRGPVGPKG EGGSGHSSRA RGEKGDAGEK GAKGSAGFGY
QGKKGEPGPP GPPGLPGPPG PATEFSVGSD GSVVSRVPGP RGPPGAPGPQ GPSGADGEPG
DPGEDGKTGP EGPPGFPGTP GDSGPKGEKG DRGEGQPGPR GPPGPPGPPG PGLRSTFVDM
EGSGYPDLES IRGLPGLPGP PGPPGPPGVA GSSTGSAASS SGAFGPAGKD GAPGQPGLPG
LPGTDGLPGA PGPQGEKGDS GELGLPGAIG EKGAQGEPGL QGPVGEPGLA GLPGPMGPVG
PPGPPGPPGP SYRVGFDDME GSGGFSNGLP GASGPPGIQG PPGLPGLPGK SGLPGLAGPK
GSEGVTGRDG RPGLDGFPGP PGQKGDRGDK GERGEAGRDG TGLRGPPGPP GPPGQIIYQT
SGNSDDAVGR VGSQGVPGIP GQAGFPGPIG PKGDRGDPGP PGYGDKGEKG EPGLVIGPDG
SVLHLEGLTG PQGDRGPSGP AGPPGPYGPP GLKGEIGMPG RPGRPGVNGY KGEKGEPGGG
YGYPGVPGPP GPPGPPGPAI PVDRFNRYDE TSRNYPAVKG EKGERGDPGL PGIPGKESDR
VDFFKKGERG DPGVKGEKGE PGGGYYDPRF GVQGPPGPPG SPGLPGPKGE SIVGPPGPQG
PPGSPGIGYD GRSGPPGPPG PPGPPGSPSL PGAYRPNYSV SIPGPPGPPG PPGIPGHSSG
ITVLRSYDTM IATARRQTEG SLIYIIDKAD LYLRVRDGLR QVMLGEYSPF FRDLENEVAE
VQPPPVILYP QSTDQSHNNG AGHYSQSGSS IRPIEPPPHP PVDPRYPPQY DPRFQDQRHT
GQTDGSLAIR NTDRYYPVTP QRRPSLPVPE PAGSDTLPSG LRIIALNAPQ TGNMRGIRGA
DFLCFQQARA VGLKGTFRAF LSSKLQDLYT IVRKSDRDSF PIVNLKDQVL FSSWESIFGD
VSKMRDNVPI YSFDGRDILR DSAWPEKMVW HGSSNKGHRQ TDHYCETWRA GDRAVTGLAS
SLQSGHLLQQ TSSSCSGSYI VLCIENAFTS PSKK
//
