ID A0AAD9DZM4_9TELE Unreviewed; 1683 AA.
AC A0AAD9DZM4;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 08-OCT-2025, entry version 8.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
DE Flags: Fragment;
GN ORFNames=P4O66_007085 {ECO:0000313|EMBL:KAK1798799.1};
OS Electrophorus voltai.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=2609070 {ECO:0000313|EMBL:KAK1798799.1, ECO:0000313|Proteomes:UP001239994};
RN [1] {ECO:0000313|EMBL:KAK1798799.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB-2022 {ECO:0000313|EMBL:KAK1798799.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1798799.1};
RA Bian C.;
RT "Electrophorus voltai genome.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK1798799.1}.
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DR EMBL; JAROKS010000012; KAK1798799.1; -; Genomic_DNA.
DR Proteomes; UP001239994; Unassembled WGS sequence.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP001239994};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1683
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042226650"
FT DOMAIN 157..279
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 79..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..497
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..519
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..742
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..936
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..965
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1082
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1442
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 172..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT NON_TER 1683
FT /evidence="ECO:0000313|EMBL:KAK1798799.1"
SQ SEQUENCE 1683 AA; 174233 MW; 33D5D95A2E47246A CRC64;
MELSVFLLML TELLTEAQRS AENETSTVGE APRTENVTKL GAEISSVTSE IKKSVEILDQ
NVTAVVSAVT TATTPDLLKA QGPTMTGNDQ SLQGMVDDSG SEGSSGLGSE FIVGVEQEKT
TKPTSLPLRE VTISSFTTVG PVSTFKTSFA ETSGVQIDAP KCFPRGSDWS FCSAGAAVGF
SLPNFLNHTG VEQVVAVLHE WAWLLHSDCH HGLEWFFCLL VAPECPLAQD GAPATLLPCR
GFCELLLDSC WMVLQNSGLP VACHTLPEGP EPGRPCVLAS NYKEESGVSL LQLIGSLPPN
QVTRVEGPDG RVAYLFEGQA SAGLPARAHL PSPFYRDFSL VFHLRPISDE AGVIFAITDS
DQKLMHVGVK LSAVEGTTRR VVFYYSHPGS NKSVEVASFE VPHQPGEWSH YSLAVNQDQV
TFYGDCSTEP RVATFERSPD DLQLDMGAGI FVGQGGAADP DKFKGLISEL KIVGNPSAAE
RRCDEGNDDD DDEDYGLEDY GSGLEAQIQS SRSPSSFFEP LPPPPVSSST RSRLDTDDTA
RETGDEDDQI SVASRTIQGS KGDKGEKGDM GTLGDRGAVG PKGESGDPDQ SSPTKGGLHR
EKGDGGENGM KAYNTMPAVL QGSPGSGYPG SKGDPGPPGP PGPPGPPGPV TEVIHPGEGK
VIERLVGPLG PAGPDGPPGA PGPSGPKGDR GDPGEDGKQG PEGPPGFPGI PGIPGPKGHK
GENGEGSPGP RGPPGPPGPP GPTHLDQATF LDMEGSGFHD MEKWQGVRGP PGPPGPRGPP
GPSMPLILDG VEGPVRFGSP GPPGKDGLPG QPGTPGLPGS PGAPGPPGLP GSKGDCGELG
SPGESGEKGP EGTAGLQGDP GQVGRAGLPG PMGPRGPQGP PGPPGPPGPI IRVNKSSGEE
SELVIQYAPG VMGPQGPQGP QGIPGLPGVT GLPGTPGEKG REGPEGQSGI PGLDGFQGPP
GQPGKKGVKG DRGEPGQPGG PPGAPGLPGP PGPVIYSTGV PGDPGQAGFP GPVGPKGDQG
IPGLPGESVK GQKGEPGQLL GPSGSPIYID GWTGKLGPQG PPGPMGEIGI PGRPGRPGLN
GNKGEKGDSG FGPGGHRYGY PGRPGPPGPP GPPGPPGPVV PVSRGYDDSR LHYGSKGEKG
ERGAPGIPGL PGLTSSFDIY ALKNEWKGEQ GSKGQKGEPG GGQYSPHYGP GEGRLGSPGP
PGPRGESVAG PPGPPGHPGP PGIGYPGRPG TPGPAGPPGP PGPAGPGAHR PSQSINIPGP
PGPPGPPGLP GIPGQSFGVM VMRSFDTMAT ATRHHPEGTL VYVIDNTDFY VRVRDGVRKV
MLGEYTPFPS PVDSHIAVVE PPPDVLYSPD SSVIAPPPRL SPVPEGQQPE LPDPDRHPPY
DLRYSTDLRH PLPTDPRHSD PQYSGPRYSD SRYLDPRYPA PAGSAEPEPR HQPHQPHGRH
AYHSGSRYYV TPVHRPIAPE ARAPTHTHSS GPALHLIALN SPKEGDMQGI RGVDHQCFLQ
AQAAGFKSTF RAFLSSQLQD LHSIVHRNDR HHIPVVNLKD EEVFSNWESI FNASDGRMRE
NTRIYSFDGR DVLEDDAWRV LTFTLQRPFP EHLCPRLEFL FLLPSFLAGQ RSWCGTVHAS
PGSGRQTATA KHGGPTTMPS LAWPPFSETA AFSSRLHAAA PVPTLCCVWR TATLPNESLG
GGG
//
