ID A0AAE1NMM8_9EUCA Unreviewed; 1400 AA.
AC A0AAE1NMM8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
GN ORFNames=Pmani_034936 {ECO:0000313|EMBL:KAK4292283.1};
OS Petrolisthes manimaculis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Anomura;
OC Galatheoidea; Porcellanidae; Petrolisthes.
OX NCBI_TaxID=1843537 {ECO:0000313|EMBL:KAK4292283.1, ECO:0000313|Proteomes:UP001292094};
RN [1] {ECO:0000313|EMBL:KAK4292283.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB745_02 {ECO:0000313|EMBL:KAK4292283.1};
RC TISSUE=Gill {ECO:0000313|EMBL:KAK4292283.1};
RA Angst P.;
RT "Genome assemblies of two species of porcelain crab, Petrolisthes cinctipes
RT and Petrolisthes manimaculis (Anomura: Porcellanidae).";
RL Submitted (NOV-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:KAK4292283.1}.
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DR EMBL; JAWZYT010004879; KAK4292283.1; -; Genomic_DNA.
DR Proteomes; UP001292094; 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 CDD; cd07066; CRD_FZ; 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; IPR016187; CTDL_fold.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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 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:UP001292094}.
FT DOMAIN 148..268
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..775
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..935
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1009
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 153..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 161..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 198..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1400 AA; 147525 MW; C78D63E5C018E739 CRC64;
MNLREQQDKV ANLRDEAGRD EPNSSHSDYF QNHHTEINTV LEEEEEEEEE EDVRGRGKKE
EEEEEEEEEE EEEEGRRGMR RRRRGRKEIN YSGSGSGEGR SDVSVHEDYI SLDMEDDDEL
PLPRLEGSGV DLEGAPPPII PPPPMHDCRT DHCEDVGVYA CSQVEWKAAL YPNTLGQGPR
QAEPMAAKFW HQLHTIDCSK EFRFVVCSLL APPCRAGVDK PLPPCREVCE AAVDQCLPVM
TRNYLTWPDD TFNCNQLPYS HQEPCLKYRD GEVIFPQGFN QDCSKHDYEY FYDNYSYEDG
NYLDHLPTLE VDDDDEGGDD DPEPDTQGSG DDEDSTSWDI DFVPNEEEYY DYHNNPLPDP
PTLTTDIPST TTTTTTTTPP SLTTTTSTTP PTPTPTSTPK IRYAPAPTPL LPLPTERQPT
NGEFGAGYLL GNEIVDESFN FRGMKGERGE KGVRGPKGRP GESITGPPGP PGPPGLPGSP
AKSWPDAGDD ILGPEPDIFL GGGRRRRPGV DFLGSCLCNE TQLVASVLAQ IPHGLPGPEG
KPGRDGLPGS HGVPGQPGRT GERGPKGEQG EKGERGHPGR SGHEGVQGAK GEAGVDGVPG
TPGPAGPQGP PGQPGWGNSG FDGLRGPSGP PGPKGEPGVP GLSGVSGSPG FPTVPGPKGE
KGDKGDKGKG FPGPPGPPGI LTDKDRNDII KQLVDTLDTK SGSFALPGGG ISIWDSSSGT
PWNRVSDDED LVNSEEGSGV LLYHPFHPKE GRSPGGPPGP PGPRGPQGIE GIPGLMGPPG
GPGDKGDAGL PGIPGIKGEH GDSGSNGLKG EVGPAGPLGE KGDRGMPGSP GQVTTLVMPD
GTNATVVKGE KGDRGRRGKR GRRGPTGSPG PTGDLGLPGW PGVTGRPGPP GPPGYGKKGD
RGSPGLPGPP GPPVQGGLLN GILGSSSSDV SQGLSTATPA REGPPGPPGP PGPPGAPGPP
GPHGSQGLPG TSPSEDNQMY IPVPGPPGPT GPQGPPGPPG VTVEGPQGPR GLEGRPGKGL
PGEPGSPGPP GATGFGSRGP PGAPGKDGLP GAGSSGNIMG GALTFPSMAA MLRMTETSPL
GTFAFLLDEE SVLVRISTGW QYISLGQVVR QPPATTRTPT TTTTTTTTAT TTTTSTAPTT
STAPTTLTTI SHASAPALAT IPAPYFAPGP PPLQVDSLVN TVDGPRLRLA ALNEPYSGDM
HGVRDTDYEC YRQARQAGLR GTFRAFLTSR VQDLDSIVRR SDHILPVVNI KGEVLFNSWR
EIFSGNGGEF SQRPRIFSFN GKEILSSRDW PQKYVWHGSD LAGVRSMSLY CDAWNSESKD
VYGLASSLLK NRLLAQERRS CNNVFAVLCI EATSEAQRRR QREAKAGGRY RRDNKLIEEY
EELLDSMDST DLELLESRGL
//
