ID A0A3P9NT68_POERE Unreviewed; 650 AA.
AC A0A3P9NT68;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein PALS1 {ECO:0000256|ARBA:ARBA00024392};
DE AltName: Full=Protein associated with Lin-7 1 {ECO:0000256|ARBA:ARBA00031033};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000012779.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000012779.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000012779.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR RefSeq; XP_008395705.1; XM_008397483.2.
DR AlphaFoldDB; A0A3P9NT68; -.
DR STRING; 8081.ENSPREP00000012779; -.
DR Ensembl; ENSPRET00000012912.1; ENSPREP00000012779.1; ENSPREG00000008665.1.
DR GeneID; 103457392; -.
DR KEGG; pret:103457392; -.
DR CTD; 100422734; -.
DR GeneTree; ENSGT00940000156087; -.
DR OMA; EQQGKLW; -.
DR OrthoDB; 2873706at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000008665; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12036; SH3_MPP5; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.287.650; L27 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR015145; L27_N.
DR InterPro; IPR035601; MPP5_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF71; PROTEIN PALS1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF09060; L27_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 107..164
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 166..222
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 234..314
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 323..395
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 454..635
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73811 MW; 8B9E120AB88FC96A CRC64;
MIASRTNGYV QEASAPAVSH RERAVDCPGQ EGSLNKSPHC SSHMERIQHY QEELRKRREE
EGKGRHDIDP NASLRLKKLS ENPKIGIDNP TFEGKEKATN KVTCLDPVVE LEELLQVLKW
VQHSLSDSQS QQDVEAITQL LAKEEFRNAY TIYSVLSQQT SRISPTSPLT VQAQDLCQEV
QRILQTSQQK EGLELSALLT NPHLQALMQA HDSVAVQEIA EESVTQYLGE TVKLVRLQKA
RDTPLGATVR NDMDNVVVSR VVKGGAAERS GLLSEGDEIL EINGIPIRGK HINEVHDLLQ
EMQGTLTFLL IPSSHNKPAP HRQTVMHVRA YFDYDPSDDP FVPCRELGLS FRKGDVLHVI
SQDDPNWWQA YRDGDEDNQP LAGLIPGKSF QQQRESLKKT TPDKSREQQG KIWCSKKSKK
LRRRNTSTLT RNTDYNDVLT YEEMSLYHQP ANRKRPVALV GPANSGHDEL RRRLLSLEPD
KFAVAVPHTT RSPRIHERNG REYHFVSRSS FEADLAAGKF IESGEYEKNL YGTSTDSVRH
VVNSGRVCLL CLHTRSLQVL RSSNLKPYVV FIAPPSQERL RTLLATEGKT LKPEELKEVT
EKAREMELNY SHFFDATVVN FDPDQVFQEL RRLVDKLDTE PQWVPSSWLC
//
