ID A0A6P7HCI1_9TELE Unreviewed; 1533 AA.
AC A0A6P7HCI1;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen type XVIII alpha 1 chain a isoform X2 {ECO:0000313|RefSeq:XP_028249446.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_028249446.1};
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_028249446.1};
RN [1] {ECO:0000313|RefSeq:XP_028249446.1}
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_028249446.1; XM_028393645.1.
DR GeneID; 114426317; -.
DR CTD; 564123; -.
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_028249446.1};
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..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..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 1044..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..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 1533 AA; 158601 MW; 4333413EEBBF7DD8 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 TSRNYPVKGE KGERGDPGLP GIPGKESDRV
DFFKKGERGD PGVKGEKGEP GGGYYDPRFG VQGPPGPPGS PGLPGPKGES IVGPPGPQGP
PGSPGIGYDG RSGPPGPPGP PGPPGSPSLP GAYRPNYSVS IPGPPGPPGP PGIPGHSSGI
TVLRSYDTMI ATARRQTEGS LIYIIDKADL YLRVRDGLRQ VMLGEYSPFF RDLENEVAEV
QPPPVILYPQ STDQSHNNGA GHYSQSGSSI RPIEPPPHPP VDPRYPPQYD PRFQDQRHTG
QTDGSLAIRN TDRYYPVTPQ RRPSLPVPEP AGSDTLPSGL RIIALNAPQT GNMRGIRGAD
FLCFQQARAV GLKGTFRAFL SSKLQDLYTI VRKSDRDSFP IVNLKDQVLF SSWESIFGDV
SKMRDNVPIY SFDGRDILRD SAWPEKMVWH GSSNKGHRQT DHYCETWRAG DRAVTGLASS
LQSGHLLQQT SSSCSGSYIV LCIENAFTSP SKK
//
