ID A0AAE1KJW5_PETCI Unreviewed; 1382 AA.
AC A0AAE1KJW5;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
GN ORFNames=Pcinc_020349 {ECO:0000313|EMBL:KAK3874733.1};
OS Petrolisthes cinctipes (Flat porcelain crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Anomura;
OC Galatheoidea; Porcellanidae; Petrolisthes.
OX NCBI_TaxID=88211 {ECO:0000313|EMBL:KAK3874733.1, ECO:0000313|Proteomes:UP001286313};
RN [1] {ECO:0000313|EMBL:KAK3874733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB745_01 {ECO:0000313|EMBL:KAK3874733.1};
RC TISSUE=Gill {ECO:0000313|EMBL:KAK3874733.1};
RA Angst P.;
RT "Genome assemblies of two species of porcelain crab, Petrolisthes cinctipes
RT and Petrolisthes manimaculis (Anomura: Porcellanidae).";
RL Submitted (OCT-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:KAK3874733.1}.
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DR EMBL; JAWQEG010002069; KAK3874733.1; -; Genomic_DNA.
DR Proteomes; UP001286313; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR CDD; cd07066; CRD_FZ; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF5; COLLAGEN TYPE XIII ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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 SUPFAM; SSF56436; C-type lectin-like; 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:UP001286313}.
FT DOMAIN 68..188
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..309
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..633
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..751
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..862
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..949
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..989
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1020
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 73..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 81..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 118..156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1382 AA; 143996 MW; C892D6CD78A30ECA CRC64;
MRKKLRGDDF YSGSGSGEGR SDVSVHEDYI SLDMEDDDEL PLPRLEGSGV DLEGAPPPII
PPPPMHDCRT DHCEDVGVFA CSQVEWKAAL YPNTLGQGPR QAEPMASKFW HQLHTIDCSK
EFRFVVCSLL APPCRAGVNK PLPPCREVCE AAVDQCLTVM TRNYLTWPDD TFNCNQLPYS
HQEPCLKYRD GEVIFPQGFN QDCSKHDYEY FYDNYSYEDG NYLDHLPTLE VEDDDEGGDD
DPEPDTQGSG DDEDSTSWDI DFVPNEEEYY DYHNNPLPGP PTLTTDLPST TTTTTTTTTP
PSLTTTTTTP PTPIPTLTPK IRFAPAPTPL LPLPTEPQPT TGEFGAGYLL GNEIVDESFN
FRGMKGERGE KGVRGPKGRP GESITGPPGP PGPPGPAGSG SSVKSWPDAG DDILGPEPDI
FLGGGRRRRP GVDFLGSCLC NETQLVASVL AQIPHGLPGP EGKPGRDGLP GSHGVPGQPG
RTGERGPKGE QGEKGERGHP GRSGHEGVQG AKGEAGVDGV PGTPGPAGPQ GPPGQPGWGN
SGFDVENGMS MAPARPGTPG TPGEKGEQGA TGVRGPRGYP GNKGERGYPG RDGEKGDRGL
RGPSGPPGPK GEPGVPGLSG VSGSPGFPTV PGPKGKKGDK GDKGEGLPGP PGPPGILTEK
DRNDIIKQLV DTLDTKSGGF ALPEGGINIW DSSSGTPWTR VSDDEDLVNS EEGSGVLLYH
PFHPKEGRSL RGPPGPPGPK GPQGIEGIPG LMGPPGGPGD KGDPGLPGIH GIKGERGDSG
SNGLTGEVGP AGPRGEKGDR GMPGSPGQVT TLVLPDGTNA TVVKGEKGDR GRRGKRGRRG
PTGSPGPTGD LGLPGWPGVT GRPGPPGPPG YGKKGDSGSP GLPGPPGPPA QGGLLNGILG
SSSSDVSQGL STATPAREGP PGPPGPPGPP GAPGPPGPQG SQGLPGTSPS EDNQMYIPVP
GPPGPTGPQG PPGPPGVTVE GPQGPRGPEG SPGKGLPGEP GSPGPPGATG FGSRGGGYGG
IDTLRQMTGH RGNRGPPGAP GKDGLPGAGP SGNIMGGALT FPSKAAMLRM TETSPLGTFA
FLLDEESVLV RISTGWQYIS LGQVVRQPPA TTRTPTTTTT TTTTTTTTST APTTSTAPTT
LTTISHASAP ALATIPAPYF APGPPPLQLR LAALNEPYSG DMHGVRDTDY ECYRQARQAG
LRGTFRAFLT SRVQDLDSIV RRSDHILPVV NIKGEVLFNS WQEIFSGNGG EFSQRPRIFS
FNGKEILSSR DWPQKYVWHG SDLAGVRSMS LYCDAWNSES KDVYGLASSL LKNRLLAQER
RSCNNVFAVL CIEATSEAQR RRQREAKAGG RYRRDNKLIE EYEELLDSMD STDLELLESR
GL
//
