EM55_MOUSE
ID EM55_MOUSE Reviewed; 466 AA.
AC P70290;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=55 kDa erythrocyte membrane protein;
DE Short=p55;
DE AltName: Full=Membrane protein, palmitoylated 1;
GN Name=Mpp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129, and C57BL/6 X CBA;
RX PubMed=8954807; DOI=10.1006/geno.1996.0621;
RA Elder B., Kuo K., Gitschier J., Kim A., Chishti A., Metzenberg A.;
RT "cDNA sequence and genomic structure of the murine p55 (Mpp1) gene.";
RL Genomics 38:231-234(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH WHRN, AND SUBCELLULAR LOCATION.
RX PubMed=16829577; DOI=10.1073/pnas.0600923103;
RA Mburu P., Kikkawa Y., Townsend S., Romero R., Yonekawa H., Brown S.D.;
RT "Whirlin complexes with p55 at the stereocilia tip during hair cell
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10973-10978(2006).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH PALS1 AND WHRN, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT "MPP1 links the Usher protein network and the Crumbs protein complex in the
RT retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19897731; DOI=10.1073/pnas.0906761106;
RA Quinn B.J., Welch E.J., Kim A.C., Lokuta M.A., Huttenlocher A., Khan A.A.,
RA Kuchay S.M., Chishti A.H.;
RT "Erythrocyte scaffolding protein p55/MPP1 functions as an essential
RT regulator of neutrophil polarity.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19842-19847(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-57 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:19897731}.
CC -!- SUBUNIT: Heterodimer with PALS1. Interacts with DLG5 and NF2. Interacts
CC (via guanylate kinase-like domain) with WHRN (via third PDZ domain).
CC {ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}.
CC -!- INTERACTION:
CC P70290; Q80VW5: Whrn; NbExp=4; IntAct=EBI-8315951, EBI-7417603;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00013};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q00013}. Cell projection,
CC stereocilium {ECO:0000269|PubMed:16829577,
CC ECO:0000269|PubMed:17584769}. Note=Colocalizes with WHRN at
CC stereocilium tip during hair cell development (PubMed:16829577).
CC Colocalizes with PALS1 in the retina, at the outer limiting membrane
CC (OLM) (PubMed:17584769). Colocalizes with WHRN in the retina, at the
CC outer limiting membrane (OLM), outer plexifirm layer (OPL), basal
CC bodies, and at connecting cilium (CC) (PubMed:17584769). Colocalizes
CC with NF2 in non-myelin-forming Schwann cells (By similarity).
CC {ECO:0000250|UniProtKB:Q00013, ECO:0000269|PubMed:16829577,
CC ECO:0000269|PubMed:17584769}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the erythrocytes (at
CC protein level). {ECO:0000269|PubMed:19897731}.
CC -!- DEVELOPMENTAL STAGE: During development of the retina, expression is
CC highest in the inner, neuroblastic layer, while at later stages it is
CC also present in the photoreceptor cell layer. Detected in the eye from
CC 14.5 dpc onwards. Highly expressed in the liver and primitive gut, and
CC at lower levels in the umbilical vein, the ventricular layer of the CNS
CC and upper/lower jaw region. At 14.5 dpc and 16.5 dpc, expression in the
CC liver and stomach is maintained. In addition, expression is present in
CC bone structures (e.g. zygomatic bone, lower jawbone), cranial nerve
CC ganglia [e.g. trigeminal (V) ganglion] and cochlea. The expression in
CC the eye is seen in the neuroblastic layer. At 16.5 dpc and 18.5 dpc, a
CC slightly higher expression is seen in the neuroblastic layer. At 16.5
CC dpc, strong expression in the upper part of the gut is maintained and
CC with the onset of ossification, expression is seen in all bone
CC structures of the body. At P7 and P90, expression in the eye is seen in
CC the ganglion cell layer, the inner nuclear layer (INL) and
CC photoreceptor cell layer. {ECO:0000269|PubMed:17584769}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q00013}.
CC -!- DISRUPTION PHENOTYPE: Neutrophils form multiple transient pseudopods
CC upon chemotactic stimulation, and do not migrate efficiently in vitro.
CC {ECO:0000269|PubMed:19897731}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; U38196; AAC52970.1; -; mRNA.
DR EMBL; BC013444; AAH13444.1; -; mRNA.
DR CCDS; CCDS30236.1; -.
DR RefSeq; NP_032647.1; NM_008621.3.
DR AlphaFoldDB; P70290; -.
DR SMR; P70290; -.
DR BioGRID; 201480; 3.
DR DIP; DIP-61219N; -.
DR IntAct; P70290; 3.
DR MINT; P70290; -.
DR STRING; 10090.ENSMUSP00000033775; -.
DR iPTMnet; P70290; -.
DR PhosphoSitePlus; P70290; -.
DR SwissPalm; P70290; -.
DR EPD; P70290; -.
DR jPOST; P70290; -.
DR PaxDb; P70290; -.
DR PeptideAtlas; P70290; -.
DR PRIDE; P70290; -.
DR ProteomicsDB; 277581; -.
DR Antibodypedia; 419; 349 antibodies from 33 providers.
DR DNASU; 17524; -.
DR Ensembl; ENSMUST00000033775; ENSMUSP00000033775; ENSMUSG00000031402.
DR GeneID; 17524; -.
DR KEGG; mmu:17524; -.
DR UCSC; uc009tpp.1; mouse.
DR CTD; 4354; -.
DR MGI; MGI:105941; Mpp1.
DR VEuPathDB; HostDB:ENSMUSG00000031402; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000158744; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; P70290; -.
DR OMA; QAPNAMT; -.
DR OrthoDB; 95102at2759; -.
DR PhylomeDB; P70290; -.
DR TreeFam; TF314263; -.
DR BioGRID-ORCS; 17524; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mpp1; mouse.
DR PRO; PR:P70290; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70290; protein.
DR Bgee; ENSMUSG00000031402; Expressed in small intestine Peyer's patch and 265 other tissues.
DR ExpressionAtlas; P70290; baseline and differential.
DR Genevisible; P70290; MM.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP: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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; SH3 domain.
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_0000094566"
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 29..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..466
FT /note="Interaction with PALS1"
FT /evidence="ECO:0000250"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00013"
SQ SEQUENCE 466 AA; 52227 MW; 8724DE75A717A464 CRC64;
MTLKSSEGEG GNSMRTALSD LYLEHLLQKR NRPETSLNQS NVTTEDMYTN GSPAPGSPAH
AKGQEARRVR LIQFEKITEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI
NGTNVTNHSV DQLQKAMKET KGMISLKVIA NQQSRLPALQ MFMRAQFDYD PQKDNLIPCK
EAGLKFVTGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS VAHSAPSEAP
SCSPFGKKKK CKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
GLLSHNPEKF AYPAPYTTRP PKKSEEDGKE YHFISTEEMT KNISANEFLE FGSYQGNMFG
TKFETVHQIH KQDKIAILDI EPQTLKTVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE
AIRSQYAHYF DLSLVNNSVD ETLKKLQEAF DQACSSPQWV PVSWVY
