ID A0A6P7HFU7_9TELE Unreviewed; 1513 AA.
AC A0A6P7HFU7;
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 X3 {ECO:0000313|RefSeq:XP_028249447.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_028249447.1};
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_028249447.1};
RN [1] {ECO:0000313|RefSeq:XP_028249447.1}
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_028249447.1; XM_028393646.1.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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_028249447.1};
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..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1285
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 467..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..558
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..694
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..752
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..819
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 97..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1513 AA; 156583 MW; 46F37DA637935826 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 TGAAGAKGEK GDKGDRGEKG
DRGPVGPKGE GGSGHSSRAR GEKGDAGEKG AKGSAGFGYQ GKKGEPGPPG PPGLPGPPGP
ATEFSVGSDG SVVSRVPGPR GPPGAPGPQG PSGADGEPGD PGEDGKTGPE GPPGFPGTPG
DSGPKGEKGD RGEGQPGPRG PPGPPGPPGP GLRSTFVDME GSGYPDLESI RGLPGLPGPP
GPPGPPGVAG SSTGSAASSS GAFGPAGKDG APGQPGLPGL PGTDGLPGAP GPQGEKGDSG
ELGLPGAIGE KGAQGEPGLQ GPVGEPGLAG LPGPMGPVGP PGPPGPPGPS YRVGFDDMEG
SGGFSNGLPG ASGPPGIQGP PGLPGLPGKS GLPGLAGPKG SEGVTGRDGR PGLDGFPGPP
GQKGDRGDKG ERGEAGRDGT GLRGPPGPPG PPGQIIYQTS GNSDDAVGRV GSQGVPGIPG
QAGFPGPIGP KGDRGDPGPP GYGDKGEKGE PGLVIGPDGS VLHLEGLTGP QGDRGPSGPA
GPPGPYGPPG LKGEIGMPGR PGRPGVNGYK GEKGEPGGGY GYPGVPGPPG PPGPPGPAIP
VDRFNRYDET SRNYPAVKGE 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
//
