ID A0A7J5Z8U5_DISMA Unreviewed; 1488 AA.
AC A0A7J5Z8U5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
GN ORFNames=F7725_009318 {ECO:0000313|EMBL:KAF3857459.1};
OS Dissostichus mawsoni (Antarctic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=36200 {ECO:0000313|EMBL:KAF3857459.1, ECO:0000313|Proteomes:UP000518266};
RN [1] {ECO:0000313|EMBL:KAF3857459.1, ECO:0000313|Proteomes:UP000518266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM0001 {ECO:0000313|EMBL:KAF3857459.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF3857459.1};
RA Park H.;
RT "Dissostichus mawsoni Genome sequencing and assembly.";
RL Submitted (MAR-2020) 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:KAF3857459.1}.
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DR EMBL; JAAKFY010000005; KAF3857459.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000518266; 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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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};
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:UP000518266};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1488
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029746615"
FT DOMAIN 140..206
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 71..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..943
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..965
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 157727 MW; 51A790CA32E8356F CRC64;
MRSRDRCSMW TLQTCILLLL LVRQTQPQRT GGGTESGGDT LRGTMLRMKT LLLLLAVFAW
SSDAWFWSKD PEPTTSTSIE SAPSGTPGAA NATQKNLEEE EEEDNLSGVG EEILNMATGI
RKFVAAWDVT PTPGTTNGGP TQKWFLCLLL APRCTAPPHP HLPCRSFCQV LQDSCWASLE
DGRLPVECHL LPDGGQEPGG PACASVSNLK EESGVSLLQL IGDPPPDEIP RVTGPRGEPG
FIFNRASVSG QPALAHVPNP FHRHFSLVFH IKPTSPGASV LFSITDGPQK IMYVGVKLSA
VQNGRQRVQF FYTEPGSEVS YEAASFEVPS MVEIWSRFSL SVFDEQVTFY QGCDSEPQVV
KFERSPDPME LDAGAGIFVG QAGGADADKF KGVILDLKVV GDHRAAERLC DDEDDSDAAS
GDFGSGDGER RQTGRTVKVN HSSSLAAGSC PPLIASQGNR LRESGTAGSK GEKGDRGIQG
LTGDLGPAGP KGSPPPRVLR VLLLLFLLSG RRTEGRKRSK VPGSVTPVIK ESAGLRGPLG
SLAPGPAAEV VRLGNGDVVQ QVSGPSGPPG FPGINGAQGP AGRTESRVPR GHKGDVGEGQ
PGPRGAPGPP GLPGTGTGDH PTFFDMEGSG FPDLDKIRGG RGRGLPGLPG PPGPPGTSVA
LGPNGPVAFG PPGPPGQDGV PGIPGPPGQP GRPGLPGPGG ERGEGGDLGL PGVAGEKQNS
QDSGFFRACI LTLLHPLRGL RVTWVCRVLR GNRGWRGFQV PWGPSDPPDL QGHQGLGTEE
VMVNPVCPVT METKEPRGHE DLQGCQEWTG SLDSRAIRET EDREESRVFQ GVTGGSGASR
APGPPGEVTY QRSDGGSGLP GRAGFPGPRG LKETKGTQGF QEMQLRGRKE SLESSWGLTG
DLSTSGVLQD GDAGPPGPEG PSGPYGASGH KGEIGIPGRP GRPGLNGVGG EKGDSGSGSG
VGYPGVPGPP GPPGPPGSYP TDRQGLLKEI KVTPDPQAEL RLQMKGESGT PGYKGDKGEP
AGGHYDPRYG VSGAGVPGAP GPPGPRGDSS VGPAGPQGPP GQPGRGYDGQ QGPPGPPGPA
GGSTPEVTEA HRLSTFLDPR DHLEHLDYLH TPQGTYDIMT ATARRQPEGS LVYIIEQTDL
YLRVRGGIRQ VQCFGFFFTY NDHYLNVHNA PYFHSHNAHY FQGNEVAAVE PPPVVPYSPH
HTDPSVHDSQ RQPESPYPSN PDPRYPSHPD PRYPSNPDPR YQPDPRFPPP TDPRFPSYTD
RLNQPDGRVS VNTAQERPAY PDSRYADPRY AVTPQRRPPP RVPHTPVHHH TSGAGLHLIA
LNSPHSGSMR GIRGADYQCF TQAQAIGMKG TFRAFLSAKL QDLHSIVRRS DRDHLPIVNL
KDEVLYDSWD AIFNEGRMKD NVPMYSFDGK DVLNDSTWPE KMLWHGSNAA GRGQVDSICE
GWRVGERALS GTAAELRSGN LLQQTPSSCS DSYVVLCIEN SYIGQAKR
//
