ID A0AAE1NMQ1_9EUCA Unreviewed; 1454 AA.
AC A0AAE1NMQ1;
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=Pmani_034936 {ECO:0000313|EMBL:KAK4292286.1};
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:KAK4292286.1, ECO:0000313|Proteomes:UP001292094};
RN [1] {ECO:0000313|EMBL:KAK4292286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB745_02 {ECO:0000313|EMBL:KAK4292286.1};
RC TISSUE=Gill {ECO:0000313|EMBL:KAK4292286.1};
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:KAK4292286.1}.
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DR EMBL; JAWZYT010004879; KAK4292286.1; -; 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 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; 1.10.2000.10; 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: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..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1198
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 661..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..818
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..989
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1016
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1063
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 1454 AA; 152989 MW; 9138592964A6A346 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 FDVENGMSMA PARPGTPGTP GEKGEQGATG VRGPRGYPGN
KGERGFPGRD GEKGDRGLRG PSGPPGPKGE PGVPGLSGVS GSPGFPTVPG PKGEKGDKGD
KGKGFPGPPG PPGILTDKDR NDIIKQLVDT LDTKSGSFAL PGGGISIWDS SSGTPWNRVS
DDEDLVNSEE GSGVLLYHPF HPKEGRSPGG PPGPPGPRGP QGIEGIPGLM GPPGGPGDKG
DAGLPGIPGI KGEHGDSGSN GLKGEVGPAG PLGEKGDRGM PGSPGQVTTL VMPDGTNATV
VKGEKGDRGR RGKRGRRGPT GSPGPTGDLG LPGWPGVTGR PGPPGPPGYG KKGDRGSPGL
PGPPGPPVQG GLLNGILGSS SSDVSQGLST ATPAREGPPG PPGPPGPPGA PGPPGPHGSQ
GLPGTSPSED NQMYIPVPGP PGPTGPQGPP GPPGVTVEGP QGPRGLEGRP GKGLPGEPGS
PGPPGATGFG SRGPPGAPGK DGLPGAGSSG NIMGGALTFP SMAAMLRMTE TSPLGTFAFL
LDEESVLVRI STGWQYISLG QVVRQPPATT RTPTTTTTTT TTATTTTTST APTTSTAPTT
LTTISHASAP ALATIPAPYF APGPPPLQVD SLVNTVDGPR LRLAALNEPY SGDMHGVRDT
DYECYRQARQ AGLRGTFRAF LTSRVQDLDS IVRRSDHILP VVNIKGEVLF NSWREIFSGN
GGEFSQRPRI FSFNGKEILS SRDWPQKYVW HGSDLAGVRS MSLYCDAWNS ESKDVYGLAS
SLLKNRLLAQ ERRSCNNVFA VLCIEATSEA QRRRQREAKA GGRYRRDNKL IEEYEELLDS
MDSTDLELLE SRGL
//
