ID A0A6P7HCI6_9TELE Unreviewed; 1419 AA.
AC A0A6P7HCI6;
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 X6 {ECO:0000313|RefSeq:XP_028249451.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_028249451.1};
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_028249451.1};
RN [1] {ECO:0000313|RefSeq:XP_028249451.1}
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}.
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DR RefSeq; XP_028249451.1; XM_028393650.1.
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; 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; 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 SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_028249451.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1419
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027916878"
FT DOMAIN 114..303
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..464
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..600
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..658
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1079
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 145483 MW; D01AE821B73384F9 CRC64;
MRTQFGVLFL LSHWVVCSDA WFWSWTGTTT LPPTVDQEGS GSPAGSGEPP SETIAHVGAE
IIDEGHGLHK TWDQTTEAPR LTTVIPPTQP ESERASEKST AGISSHTITP EDSGVSLLQL
IGDPPPNEIT RVYGTDNNPA YVFGPDANTG QLARAHFPSP FYRDFALIFN LKPTSDRGGI
IFSITDASQQ IMYVGVKLSE VQGSNQNLIL YYTEPDSQQS YEAARFLVPS MRDVWTRFAI
AVRDDKVMFY LNCDADPQVM RIERSPDEME LEGGAGVFVG QAGGADPAKF LGVIGELRVV
GDPRAAERHC EEDGDDSDMA SGEGSGYEET RPPKPGAEKH KSTTMPPSSR PIQQPPLKNE
VAMARETGAA GAKGEKGDKG DRGEKGDRGP VGPKGEGGSG HSSRARGEKG DAGEKGAKGS
AGFGYQGKKG EPGPPGPPGL PGPPGPATEF SVGSDGSVVS RVPGPRGPPG APGPQGPSGA
DGEPGDPGED GKTGPEGPPG FPGTPGDSGP KGEKGDRGEG QPGPRGPPGP PGPPGPGLRS
TFVDMEGSGY PDLESIRGLP GLPGPPGPPG PPGVAGSSTG SAASSSGAFG PAGKDGAPGQ
PGLPGLPGTD GLPGAPGPQG EKGDSGELGL PGAIGEKGAQ GEPGLQGPVG EPGLAGLPGP
MGPVGPPGPP GPPGPSYRVG FDDMEGSGGF SNGLPGASGP PGIQGPPGLP GLPGKSGLPG
LAGPKGSEGV TGRDGRPGLD GFPGPPGQKG DRGDKGERGE AGRDGTGLRG PPGPPGPPGQ
IIYQTSGNSD DAVGRVGSQG VPGIPGQAGF PGPIGPKGDR GDPGPPGYGD KGEKGEPGLV
IGPDGSVLHL EGLTGPQGDR GPSGPAGPPG PYGPPGLKGE IGMPGRPGRP GVNGYKGEKG
EPGGGYGYPG VPGPPGPPGP PGPAIPVDRF NRYDETSRNY PAVKGEKGER GDPGLPGIPG
KESDRVDFFK KGERGDPGVK GEKGEPGGGY YDPRFGVQGP PGPPGSPGLP GPKGESIVGP
PGPQGPPGSP GIGYDGRSGP PGPPGPPGPP GSPSLPGAYR PNYSVSIPGP PGPPGPPGIP
GHSSGITVLR SYDTMIATAR RQTEGSLIYI IDKADLYLRV RDGLRQVMLG EYSPFFRDLE
NEVAEVQPPP VILYPQSTDQ SHNNGAGHYS QSGSSIRPIE PPPHPPVDPR YPPQYDPRFQ
DQRHTGQTDG SLAIRNTDRY YPVTPQRRPS LPVPEPAGSD TLPSGLRIIA LNAPQTGNMR
GIRGADFLCF QQARAVGLKG TFRAFLSSKL QDLYTIVRKS DRDSFPIVNL KDQVLFSSWE
SIFGDVSKMR DNVPIYSFDG RDILRDSAWP EKMVWHGSSN KGHRQTDHYC ETWRAGDRAV
TGLASSLQSG HLLQQTSSSC SGSYIVLCIE NAFTSPSKK
//
