ID A0AAE1KJ73_PETCI Unreviewed; 1374 AA.
AC A0AAE1KJ73;
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:KAK3874734.1};
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:KAK3874734.1, ECO:0000313|Proteomes:UP001286313};
RN [1] {ECO:0000313|EMBL:KAK3874734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB745_01 {ECO:0000313|EMBL:KAK3874734.1};
RC TISSUE=Gill {ECO:0000313|EMBL:KAK3874734.1};
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:KAK3874734.1}.
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DR EMBL; JAWQEG010002069; KAK3874734.1; -; Genomic_DNA.
DR Proteomes; UP001286313; 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 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; IPR050149; Collagen_superfamily.
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; 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 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..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1117
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 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 1374 AA; 143164 MW; 95FB89E3DA3A9F9B 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 FGSRGPPGAP
GKDGLPGAGP SGNIMGGALT FPSKAAMLRM TETSPLGTFA FLLDEESVLV RISTGWQYIS
LGQVVRQPPA TTRTPTTTTT TTTTTTTTST APTTSTAPTT LTTISHASAP ALATIPAPYF
APGPPPLQVD SLVNTVDGPR LRLAALNEPY SGDMHGVRDT DYECYRQARQ AGLRGTFRAF
LTSRVQDLDS IVRRSDHILP VVNIKGEVLF NSWQEIFSGN GGEFSQRPRI FSFNGKEILS
SRDWPQKYVW HGSDLAGVRS MSLYCDAWNS ESKDVYGLAS SLLKNRLLAQ ERRSCNNVFA
VLCIEATSEA QRRRQREAKA GGRYRRDNKL IEEYEELLDS MDSTDLELLE SRGL
//
