ID A0A3Q3SZE5_9TELE Unreviewed; 1181 AA.
AC A0A3Q3SZE5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000033290.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000033290.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMAMP00000033290.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3Q3SZE5; -.
DR STRING; 205130.ENSMAMP00000033290; -.
DR Ensembl; ENSMAMT00000034149.2; ENSMAMP00000033290.1; ENSMAMG00000022394.2.
DR GeneTree; ENSGT00940000165423; -.
DR InParanoid; A0A3Q3SZE5; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005594; C:collagen type IX trimer; 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; 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:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
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 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:UP000261640};
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..1181
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018704515"
FT DOMAIN 189..309
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 29..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..138
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..532
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..609
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..805
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 241..279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1181 AA; 125180 MW; A74191833CA5BDE2 CRC64;
MLRIRSWLLL LVLCAGSLEA WFWYPDPEPT TPAPTETTKT TETGTTGATM TPNSTVKMEE
EEEEDDNLSG AGEEILTVTT GVPKVVMPWD VTNGTTNGSQ TEMVEIANSN TTGNTDRLRG
KREEGSRVGA GDGSGSGSGF RADSRSDVES VTVLRSDDVL LSNLTGDLAQ IKTLESVLDS
TPADYHVNDP DSACLPVPSD WPICSGKRSE FFTLPNFFNH TSVEEVEALL QKWAWVTRVG
CHPSAEWFLC LLLAPRCPSP ALPVYLPCRS FCHVLQDSCW ASLENGHLPV ECGLLPEARE
PRRPACVSVS NCKEESGLSL LELIGDPPPD EITKVYGPRG EAYVFTSAAV SGQPALAHIP
NPFYRHFSLL FHIKPSSPAA SVLFSITDGP QRLMYIGVKL SAVQSGRQKV QFFYTEPDSE
ASYEAASFDV PSLVNTWSRF SLSVFEDQVI FYHGCDSEPQ VVKFERSPDP MELDKAAGIF
VGQAGGADTD KFQVVGAKGE KGDNGVKGSK GDIGPAGPKG DSGSSSGASP QSGGRGQKVT
HLSGSSGFGY PGNKGERGPQ GPPGPPGPPG PAAEVVRLGD GSVVQQVAGP PGPPGSPGLD
GAAGLPGTDG EPGDPGEDGK AVRVCCSRSQ GPAGPRGSPG TQGTAGTPLL FDLLILTNSH
TWLECLFTSG TNCPNFGEKG EPGIILGPDG RSMYLGGLVG QPVKTILFYL CVSQGPPGPP
GPPGPPGPPI PVDRIGVSRN VKYSTVGEKG DRGPPGIPGV GSNFDFHTLK HELKGETGSP
GLKGEKGEPG GGFYDPRYGG IGAPGHPGPP GPKGDSIVGP PGPQGPPGHP GRGYDGQPGP
PGPPGPPGPS LPGVTVLRSY DSMTATARRQ PEGTLVYIID QTDLYLRVRD GVRQVQLGSY
IALPSEDGNE VAAVEPPPVF PYYPDQTSHS SQSSPDSPVQ PDPYQPTDPR YVANPDSRHQ
PDPRYPSPTD PRFPSYADRI NQPDVTPQRR PPPPVPQTPV HHHTSGPGLH LIAVNSPQTG
SMKGIRGADF LCFTQARAIG MKGTFRAFLS AKLQDLHSIV RKADRDSIPV VNLKDEVLFD
SWDAIFRGGR MKDNVPIYSF EGKDVLRDST WPEKMMWHGS TSAGLQHVDS FCETWRVDDR
ALTGMASSLQ SGSLLQQTSS SCSSSHAVLC VENSYMGQSK R
//
