ID A0A2U9CZX8_SCOMX Unreviewed; 456 AA.
AC A0A2U9CZX8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative partitioning defective 6-like gamma {ECO:0000313|EMBL:AWP21620.1};
GN ORFNames=SMAX5B_015855 {ECO:0000313|EMBL:AWP21620.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP21620.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21620.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PAR6 family.
CC {ECO:0000256|ARBA:ARBA00008625}.
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DR EMBL; CP026264; AWP21620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CZX8; -.
DR STRING; 52904.ENSSMAP00000012289; -.
DR OMA; RNADCNA; -.
DR OrthoDB; 5401122at2759; -.
DR Proteomes; UP000246464; Chromosome 22.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd06403; PB1_Par6; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102; PAR-6-RELATED; 1.
DR PANTHER; PTHR14102:SF3; PARTITIONING DEFECTIVE 6 HOMOLOG GAMMA; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 18..98
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT DOMAIN 159..252
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50450 MW; F6993994E4126DB0 CRC64;
MNRSFNKSQP LRNADCNAVE VKSKYGAEFR RFSVDRVKPG KFEEFYKLIL HIHRIANMEV
MIGYADIHGD LLPINNDDNF CKAVSTAHPL LRIFIQRQEE VDYANFGTNT ITRRKKAVVA
LRNNDINRKR PHIRIGMPQD FRPVSSIIDV DILPESHRRV RLYRHGSDKP LGFYIRDGTS
VRVTPHGLEK VPGIFISRMV PGGLAESTGL LAVNDEVLEV NGIEVTGKSL DQVTDMMIAN
SHNLIVTVKP VNQRNNVVRS SRISGSSGQS SDSSGSTGYP SLSVASVGVR SSVAHGYQDD
LESDEEADIV IESSLKRPSQ RSNASLASSV SRTHQQTPQT VSGLASPPSP PTRRSSMVST
ASFRSQPSLN GGSHQHQQQH SSLSYQLHRD LNLQHSLHQQ PQHSHYVQPP HHSSNPALRH
SNGSLHKILS SLKTDPRHSL ALPRGGVEED GTVITL
//
