EM55_PONAB
ID EM55_PONAB Reviewed; 466 AA.
AC Q5RDW4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=55 kDa erythrocyte membrane protein;
DE Short=p55;
DE AltName: Full=Membrane protein, palmitoylated 1;
GN Name=MPP1; Synonyms=EMP55;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential regulator of neutrophil polarity. Regulates
CC neutrophil polarization by regulating AKT1 phosphorylation through a
CC mechanism that is independent of PIK3CG activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with PALS1. Interacts with DLG5 and NF2. Interacts
CC (via guanylate kinase-like domain) with WHRN (via third PDZ domain) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00013};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q00013}. Cell projection,
CC stereocilium {ECO:0000250|UniProtKB:P70290}. Note=Colocalizes with WHRN
CC at stereocilium tip during hair cell development. Colocalizes with
CC PALS1 in the retina, at the outer limiting membrane (OLM). Colocalizes
CC with WHRN in the retina, at the outer limiting membrane (OLM), outer
CC plexifirm layer (OPL), basal bodies, and at connecting cilium (CC) (By
CC similarity). Colocalizes with NF2 in non-myelin-forming Schwann cells
CC (By similarity). {ECO:0000250|UniProtKB:P70290,
CC ECO:0000250|UniProtKB:Q00013}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q00013}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; CR857779; CAH90043.1; -; mRNA.
DR RefSeq; NP_001124975.1; NM_001131503.1.
DR AlphaFoldDB; Q5RDW4; -.
DR SMR; Q5RDW4; -.
DR STRING; 9601.ENSPPYP00000023388; -.
DR Ensembl; ENSPPYT00000024366; ENSPPYP00000023388; ENSPPYG00000020893.
DR GeneID; 100171848; -.
DR KEGG; pon:100171848; -.
DR CTD; 4354; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000158744; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q5RDW4; -.
DR OMA; QAPNAMT; -.
DR OrthoDB; 95102at2759; -.
DR TreeFam; TF314263; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR CDD; cd12080; SH3_MPP1; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR035475; MPP1_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 Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; SH3 domain; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT CHAIN 2..466
FT /note="55 kDa erythrocyte membrane protein"
FT /id="PRO_0000347219"
FT DOMAIN 71..152
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 158..228
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 282..451
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 268..466
FT /note="Interaction with PALS1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70290"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
SQ SEQUENCE 466 AA; 52265 MW; C288446F7E851419 CRC64;
MTLKASEGES GGSMHTALSD LYLEHLLQKR SRPEAVSHPL NTVTEDMYTN GSPAPGSPAQ
VKGQEVRKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI
NGTNVTNHSV DQLQKAMKET KGMISLKVIP NQQSRLPALQ MFMRAQFDYD PKKDNLIPCK
EAGLKFATGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS VAQSAPSEAP
SCSPFGKKKK YKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
ALLSQNPEKF VYPVPYTTRP PRKSEEDGKE YHFISTEEMT RNISANEFLE FGSYQGNMFG
TKFETVHQIH KQDKIAILDI EPQTLKIVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE
AIRSQYAHYF DLSLVNNGVD ETLKKLQEAF DQACSSPQWV PVSWVY
