ID A0AAE0V8R4_9TELE Unreviewed; 1678 AA.
AC A0AAE0V8R4;
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};
GN ORFNames=QTP70_014024 {ECO:0000313|EMBL:KAK3543315.1};
OS Hemibagrus guttatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Hemibagrus.
OX NCBI_TaxID=175788 {ECO:0000313|EMBL:KAK3543315.1, ECO:0000313|Proteomes:UP001274896};
RN [1] {ECO:0000313|EMBL:KAK3543315.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Male_cb2023 {ECO:0000313|EMBL:KAK3543315.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK3543315.1};
RA Bian C.;
RT "Male Hemibagrus guttatus genome.";
RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
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}.
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:KAK3543315.1}.
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DR EMBL; JAUCMX010000006; KAK3543315.1; -; Genomic_DNA.
DR Proteomes; UP001274896; 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: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:SF1070; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
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:UP001274896};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1678
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042230117"
FT DOMAIN 210..329
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 87..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..119
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..851
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..911
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1150
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1260
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 225..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 262..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1678 AA; 174702 MW; A3CF3547AEF28278 CRC64;
MLSKMPSLGL WLVLVGLCIG HSHGWFWFDE SKDNSKVTPT PAYATTLGIT LGTTLGTTSG
TTVPKTLATT EYLWTKGTDA PDVDVLAKGE EKGSGGGAEV EHGPESESDS GSWSLSGSGD
EPESGPTIKP NTLPPLTKIQ EINNVQTNLS IGGDNIHAVT EDMKLEKNLT KEDLSETDEH
IGNVASGDTI SNLLTAEGNQ SFFASEIPAT ASPRCLLVDF DLPFCHSLKN GSFIIPNFLN
QSSVEDVQSF LGEWAFLIQS DCHEAVEWFF CLLAMPSCGM PGLSPQMPCR SFCELLIDNC
WTLLQDRRLP VECSSLPEEG DDGNQCLSIS TQKAEKGVSL SQLIGYPLPD GVTRSYEPDS
GFVFDQNSKT GQLARVHLPT SFYRDFSLMF NLKPTSTKAG VIFSITDTYQ KIMYVGVKLT
PVKDGKQNIV LFYTEPDSQA SYEAASFTVP SLVNYWTRFS LSVLDDKVTL YPSCDSEPKV
LPFERSPDEM DLEPGAGIFV GQAGGADDDK FVGIIGDLKV VGDPHVAAHY CEEEEDDSDG
ASGEYGSGFY SHEHTVTTTS QPSNPLQQPP VIPTVVTVSK DVPIGYDGYG RISGSYGDSR
RTSGSHVLTG AGAQGEKGDK GDKGPKGDRG PEGPKGDAGS RVESGGGGGA KGEKGSQGEK
GMKGAAGFGY PGAKGDQGPP GPPGPPGPPG PTVDIAERGD GSVVQRVPGP RGPPGPPGFP
GPAGAEGEAG DPGEDGIAGP VGPPGFPGVP GDPGAKGEKG DKGEGNPGPR GLPGPPGPPG
PPHRSDRPTF VDMEGSGFGD LEGLQGLPGL PGPPGPPGPP GPPGPESSSA SHASVSGIPG
PSGPPGKDGT PGQPGLPGAP GSDGKPGVPG PKGEKGDTGE LGLPGAVGEK GAQGIPGPAG
PPGQTGLAGL PGPMGPVGPP GPPGPGYNVG FDDLEGSGVN VYGGVPGVRG PEGVRVSDLF
ISWVHLDYRV SLVYLGRKER KVARDSREQL AILELMAFQA HRIDDDIQGP KGERGFKGDR
GDPGRDGVGI PGPPGPPGQI IYRSPDGHDT VVDTRLSGIP GQAGFPGPMG PKGERGDPGA
PGHAIKGEKG EPGVVIGPDG SPLFLGSMVG QKGEMGPAGP VGPPGPYGHP GMKGEIGMPG
RPGRPGIIGS KGEKGEPSSG SGYGYPGAPG PPGPPGPPGR SIYPADLERF GIHEEFGRVY
PGVKGEKGDR GLPGIPGTPG NVDVFRLKNE LKGERGDPGL KGEKGEPGGH YGSPYGGVQG
PPGPPGPKGD SVRGPPGPQG PPGPSGIGYE GRAGNPGPPG PPGPPGLPSL PGAHRPTISI
PGPPGPPGPP GQSAGVTVLR TFDRLLATAQ RQPEGALFYL MDTSDLYVRV RDGVRKVMLG
DHNSFYRDSN NEVAAVQPPP VVHYPPSHSA NNEAEVYSPV DTAVRQPESP NSEHPQPGID
PQYSTHYSSH PDVRYPPQPD SRYPPRTDHH IPVPPERYPI TPIHRPSIPV HQPEGHVHTS
GPGLHLIALN SPQVGNMRGI RGADFLCFQQ ARAAGLKGTF RAFLSSKLQD LYSIVRKSDR
NTLPIVNLKD QVLFSSWESL FSDSEGRMKT NIPLYSFDGR DILRDSAWPE KMIWHGSSGK
GHRQMDNYCE TWRTSDHAVM GLASSLQAGQ LLQQKPSSCS NSFIVLCIEN SYITQSKK
//
