ID U3HZE1_ANAPP Unreviewed; 722 AA.
AC U3HZE1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Protein PALS1 {ECO:0000256|ARBA:ARBA00024392};
DE AltName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
DE AltName: Full=Protein associated with Lin-7 1 {ECO:0000256|ARBA:ARBA00031033};
GN Name=PALS1 {ECO:0000313|Ensembl:ENSAPLP00000000361.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000000361.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000000361.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000000361.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; U3HZE1; -.
DR STRING; 8840.ENSAPLP00000000361; -.
DR Ensembl; ENSAPLT00000000929.2; ENSAPLP00000000361.2; ENSAPLG00000000613.2.
DR GeneTree; ENSGT00940000156087; -.
DR HOGENOM; CLU_001715_5_4_1; -.
DR Proteomes; UP000016666; Chromosome 5.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0035750; P:protein localization to myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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:SF14; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 120..177
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 179..235
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 256..336
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 345..417
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 479..660
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 82396 MW; 240834C7E4D886A1 CRC64;
MTTSHMNGHI TEDSDSETKN VDLASPEEPQ KHREMAVDCP GDLGSRMMPM RRSAQLERIR
QQQEDMRRRR EEEGKKQELD LTASMRLKKL AQIPPKTGID NPIFDTEEGI VLESPHYTVK
TLEVEELLTS LKHIQHILVD PQSQEDISLI LQLVQNTDFQ NAFKIHNAVT VHMNKASPPY
PLISNAQELA QEVQSVLKPS HHKDGQELNA LLNAPHMQAL LLAHDKVAEQ EMQPEPVTDE
RIYENVGTYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
VLEINGIEIR GKDVNEVFDL LADMHGTLTF VLIPSQQSKP PPAKETVIHV KAHFDYDPSD
DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYRDGDEDN QPLAGLIPGK SFQQQREAMK
QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR
PIVLIGPQNC GQNELRQRLM NNEVDRFASA VPHTTRSRRE TEVAGRDYHF ISRQAFENDI
AAGKFIEYGE FEKNLYGTSI DSVRQVINSG KICLLNLHTQ SLKTLRNSDL KPYIIFVAPP
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN
KLDTEPHESW KSSSCCFAGC VKDAVTHQCP RCSPYLSHWM RGVRREQTAE RNCRPEKTAI
LL
//
