ID A0AA88PLM4_9TELE Unreviewed; 1507 AA.
AC A0AA88PLM4;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
GN ORFNames=Q8A67_014401 {ECO:0000313|EMBL:KAK2889026.1};
OS Cirrhinus molitorella (mud carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Cirrhinus.
OX NCBI_TaxID=172907 {ECO:0000313|EMBL:KAK2889026.1, ECO:0000313|Proteomes:UP001187343};
RN [1] {ECO:0000313|EMBL:KAK2889026.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Prfri {ECO:0000313|EMBL:KAK2889026.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2889026.1};
RA Liu H.;
RT "Chromosome-level Genome Assembly of mud carp (Cirrhinus molitorella).";
RL Submitted (AUG-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:KAK2889026.1}.
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DR EMBL; JAUYZG010000014; KAK2889026.1; -; Genomic_DNA.
DR Proteomes; UP001187343; 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:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 4.
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:UP001187343};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1507
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041671218"
FT DOMAIN 167..289
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 487..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..657
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1054
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1071
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 182..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1507 AA; 158427 MW; C5026A43A29EB8B9 CRC64;
MRFNWGLSLL LILYVSPLTA SFWWNSSPVT KAPTVDNDTS VNGTTRKDEN ITDVGSEILD
LAKGIQGFVK NWDQNSTVNW NNSVTVTTPV ISSKPGHSKT GNDKSLSEDL EHEMNVKASS
GDAIGSGLGS GPTLDLAQEG KTTATNLTGT RVTDSRISII STSAYHKDST NCLPRGSDWP
FCLSHGEVTF SVPNFFNHTQ AEDVVAVLNE WGWLLRSGCH HGLEWFFCLL LAPRCHQPSE
KSGIALLPCR TFCEVLLDSC WTVLQERGLP VACHTLPEGP EPSQPCLTVS NHKEESGIAL
LQLLGTFPPE DITRVPGPNG QTAYYFTKDT NTEQMARAHL PTPFYRDFSI VFHLKPTSED
AGVLFSITDS NQKIMYLGVK LSAVEDGKRK VIFYYTEPDS DTSQEVARFE VEHKPQEWSR
FSLAVSLDQV SFYEDCESEP KVVKFERSPD DLLLETNSKI FVGQSGADDP DKYEGLISEL
RVVGNPRTAE RPCNDADDDD DDYDASGDNG SGIEDRINMK LNLGSVQLPL PPQPDSTGHE
NTDKMRDSKL NSSTLSGSGG THENKGDDQE KEMQLNIGSG LPGPKGDRGP PGPPGPPGPQ
GPVTELIVTG DEKVARVQGP IGPQGPEGPP GKEGPQGEPG EPGQDGRPGP EGPRGFQGAT
GSAGPKGQKG QKGEGHPGPR GPPGPPGPPG PSISDKTGLC CQPGLPGPPG PPGPPGPDWA
TESELESLES GPTGPPGQNG LPGRPGPPGR PGKPGPPGPP GQKGDCGEIG LNGVTGERQS
PFSAFSFLSS WFPSWETNGE QGPQGSSGIP GLEGMPGLPG PMGPQGPQGP PGPPGPPGPA
FQITTDGNKT EVDLQYIPGV MGPPGPQGPQ GIPGLPGKSG LPGIPGQKGQ EGERGREGIP
GLDGFPGKIG LKGERGWKGD KGDPGRAVGP PGLPGPPGPP GQVIYINGSE NGEYGIPGPQ
GEPGIAGQAG FPGPMGPKGD QGERGIQGDS IKGQKGEPGL IVDSRGSPIS LEWLSELVAG
PPGPEGPVGP VGKPGTKGEI GLPGRPGRPG LNGKKGAKGD SGGGYGYGYQ GPPGPPGPPG
PPGPPVSVGR YDGYDDGSSR FPYAFKGDKG ERGAPGIPGL PGLTTTFDIY AFKHEMKGEL
GSKGQKGEPG LGYYEPYHSG AQSLPGRPGP PGPRGESIIG PPGPPGPPGA PGIGYDGRPG
SPGPPGPPGP SGSLLPGAHR PSQTISIPGP PGPPGPPGPP GHLTGVMVLR SVDTMDSTTI
RYPEGTLIYV KDNRELYMRV QDGIREVMLG EYTPFPKGLD NQMEAVEPPQ VVQYSQDYPT
TSPQQAPPQP EAQYPLHLIA LNSPQLGNMQ GIRGIDHQCF LQAQAIGLKG TFRAFLSSQL
QDLHSIVRQN DRESLPIVNL QDEELFSNWE SIFSGSEGKM NDDVRIYSFD GRDVLNDDAW
PEKMVWHGSN THGNRQTDSF CETWRTGSHA VTGMASSLQE GYLLQQLPRG CTSSFIVLCI
ENSYIAE
//
