EM55_BOVIN
ID EM55_BOVIN Reviewed; 466 AA.
AC Q17QN6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=55 kDa erythrocyte membrane protein;
DE Short=p55;
DE AltName: Full=Membrane protein, palmitoylated 1;
GN Name=MPP1; Synonyms=EMP55;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PALS1.
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).
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). Interacts with PALS1. {ECO:0000250,
CC ECO:0000269|PubMed:17584769}.
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; BC118256; AAI18257.1; -; mRNA.
DR RefSeq; NP_001068952.1; NM_001075484.1.
DR AlphaFoldDB; Q17QN6; -.
DR SMR; Q17QN6; -.
DR STRING; 9913.ENSBTAP00000017340; -.
DR PaxDb; Q17QN6; -.
DR PRIDE; Q17QN6; -.
DR Ensembl; ENSBTAT00000017340; ENSBTAP00000017340; ENSBTAG00000013046.
DR GeneID; 510998; -.
DR KEGG; bta:510998; -.
DR CTD; 4354; -.
DR VEuPathDB; HostDB:ENSBTAG00000013046; -.
DR VGNC; VGNC:31582; MPP1.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000158744; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q17QN6; -.
DR OMA; QAPNAMT; -.
DR OrthoDB; 95102at2759; -.
DR TreeFam; TF314263; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000013046; Expressed in jejunum and 105 other tissues.
DR ExpressionAtlas; Q17QN6; baseline.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; 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 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_0000286142"
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 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 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; 52184 MW; 401F718FBD609ABD CRC64;
MTLKASEGEG GGGMRTALSD LYLEHLLQKH NRPEPVSPQL SAVMEDMYTN GPAALGSPAQ
TQGQEARKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL HGGMVHRQGS LHVGDEILEI
NGTNVTNHSV DQLQKAMKET KGMISLKVIP NQQNRLPALQ MFMRAQFDYD PRKDNLIPCK
EAGLKFLTGD VIQIINKDDS NWWQGRVEGS SQESAGLIPS PELQEWRVAS GAHSAPSEAP
SCSPFGKKKK YKDKYLAKHS AIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKS
ALLSQNPDKF AYPAPYTTRP ARKSEEDGKE YHFISTEEMT RSISANEFLE FGSYQGNMFG
TKFETVHQIH KQDKVAILDI EPQTLKIVRT AELSPFIVFI APTDQGTQTD TLQQLQKDSE
AIRSQYAHYF DLSLVNNSVE ETLKTLQETF DQACRSPQWV PVSWVY
