PKHB1_MOUSE
ID PKHB1_MOUSE Reviewed; 243 AA.
AC Q9QYE9; Q9QYB3; Q9QYB4; Q9QYD2; Q9QYD3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pleckstrin homology domain-containing family B member 1;
DE Short=PH domain-containing family B member 1;
DE AltName: Full=Evectin-1;
DE AltName: Full=PH domain-containing protein in retina 1;
DE Short=PHRET1;
DE AltName: Full=Pleckstrin homology domain retinal protein 1;
GN Name=Plekhb1; Synonyms=Evt1, Phr1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain, and Retina;
RX PubMed=10585447; DOI=10.1074/jbc.274.50.35676;
RA Xu S., Ladak R., Swanson D.A., Soltyk A., Sun H., Ploder L., Vidgen D.,
RA Duncan A.M.V., Garami E., McInnes R.R., Valle D.;
RT "PHR1 encodes an abundant, pleckstrin homology domain-containing integral
RT membrane protein in the photoreceptor outer segments.";
RL J. Biol. Chem. 274:35676-35685(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP INTERACTION WITH MYO1C AND MYO7A, AND HOMODIMERIZATION.
RX PubMed=15976448; DOI=10.1242/jcs.02424;
RA Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G.,
RA Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C.;
RT "PHR1, an integral membrane protein of the inner ear sensory cells,
RT directly interacts with myosin 1c and myosin VIIa.";
RL J. Cell Sci. 118:2891-2899(2005).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15456885; DOI=10.1128/mcb.24.20.9137-9151.2004;
RA Xu S., Wang Y., Zhao H., Zhang L., Xiong W., Yau K.W., Hiel H.,
RA Glowatzki E., Ryugo D.K., Valle D.;
RT "PHR1, a PH domain-containing protein expressed in primary sensory
RT neurons.";
RL Mol. Cell. Biol. 24:9137-9151(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20301200; DOI=10.1002/lary.20779;
RA Tan B., Brown D., Xu S., Valle D.;
RT "PHR1 is a vesicle-bound protein abundantly expressed in mature olfactory
RT neurons.";
RL Laryngoscope 120:1002-1010(2010).
RN [8]
RP STRUCTURE BY NMR OF 22-138.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of pleckstrin homology domain-
RT containing protein family B member 1 from mouse.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- SUBUNIT: Binds transducins (By similarity). Homodimer. Interacts (via
CC PH domain) with MYO1C. Interacts (via PH domain) with MYO7A.
CC {ECO:0000250|UniProtKB:Q9UF11, ECO:0000269|PubMed:15976448}.
CC -!- INTERACTION:
CC Q9QYE9-1; Q9WTI7: Myo1c; NbExp=4; IntAct=EBI-1127141, EBI-777558;
CC Q9QYE9-2; Q9WTI7: Myo1c; NbExp=2; IntAct=EBI-1127145, EBI-777558;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20301200}. Cytoplasm
CC {ECO:0000269|PubMed:20301200}. Note=Membrane-associated. Highly
CC expressed in the outer segments of photoreceptor cells, both in rods
CC and cones (By similarity). Localizes to the apical juxta-nuclear Golgi
CC region of the cytoplasm (PubMed:20301200).
CC {ECO:0000250|UniProtKB:Q9UF11}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9QYE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYE9-2; Sequence=VSP_009782;
CC Name=3;
CC IsoId=Q9QYE9-3; Sequence=VSP_009781;
CC Name=4;
CC IsoId=Q9QYE9-4; Sequence=VSP_009781, VSP_009782;
CC -!- TISSUE SPECIFICITY: Highly expressed in retina and brain. In retina,
CC abundantly expressed in photoreceptors. Isoform 4 is the predominant
CC isoform expressed in mature olfactory receptor neurons and vestibular
CC and cochlear hair cells. Also expressed in cells with possible sensory
CC function, including peripheral retinal ganglion cells, cochlear
CC interdental cells, and neurons of the circumventricular organ (at
CC protein level). {ECO:0000269|PubMed:10585447,
CC ECO:0000269|PubMed:15456885, ECO:0000269|PubMed:20301200}.
CC -!- DISRUPTION PHENOTYPE: Mice appear normal at birth with no obvious
CC behavioral or growth abnormalities nor overt sensory deficits. At 6
CC months and 1 year of age, mice display normal retinal histology and
CC normal response in electroretinograms. {ECO:0000269|PubMed:15456885}.
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DR EMBL; AF071000; AAD32952.1; -; mRNA.
DR EMBL; AF000272; AAF16676.1; -; mRNA.
DR EMBL; AF071001; AAF16683.1; ALT_TERM; Genomic_DNA.
DR EMBL; AF101053; AAF18571.1; -; mRNA.
DR EMBL; AF100613; AAF18933.1; -; mRNA.
DR EMBL; AK005102; BAB23819.1; -; mRNA.
DR EMBL; BC024756; AAH24756.1; -; mRNA.
DR CCDS; CCDS21504.1; -. [Q9QYE9-1]
DR CCDS; CCDS52324.1; -. [Q9QYE9-4]
DR CCDS; CCDS52325.1; -. [Q9QYE9-3]
DR CCDS; CCDS52326.1; -. [Q9QYE9-2]
DR RefSeq; NP_001156654.1; NM_001163182.1. [Q9QYE9-2]
DR RefSeq; NP_001156655.1; NM_001163183.1. [Q9QYE9-3]
DR RefSeq; NP_001156656.1; NM_001163184.1. [Q9QYE9-4]
DR RefSeq; NP_001156657.1; NM_001163185.1. [Q9QYE9-4]
DR RefSeq; NP_001156658.1; NM_001163186.1. [Q9QYE9-3]
DR RefSeq; NP_001156659.1; NM_001163187.1. [Q9QYE9-4]
DR RefSeq; NP_001278265.1; NM_001291336.1.
DR RefSeq; NP_038774.1; NM_013746.3. [Q9QYE9-1]
DR RefSeq; XP_006507969.1; XM_006507906.1. [Q9QYE9-3]
DR PDB; 2D9V; NMR; -; A=22-138.
DR PDBsum; 2D9V; -.
DR AlphaFoldDB; Q9QYE9; -.
DR SMR; Q9QYE9; -.
DR BioGRID; 205156; 6.
DR IntAct; Q9QYE9; 2.
DR MINT; Q9QYE9; -.
DR STRING; 10090.ENSMUSP00000078175; -.
DR iPTMnet; Q9QYE9; -.
DR PhosphoSitePlus; Q9QYE9; -.
DR MaxQB; Q9QYE9; -.
DR PaxDb; Q9QYE9; -.
DR PRIDE; Q9QYE9; -.
DR ProteomicsDB; 289504; -. [Q9QYE9-1]
DR ProteomicsDB; 289505; -. [Q9QYE9-2]
DR ProteomicsDB; 289506; -. [Q9QYE9-3]
DR ProteomicsDB; 289507; -. [Q9QYE9-4]
DR Antibodypedia; 30966; 46 antibodies from 22 providers.
DR DNASU; 27276; -.
DR Ensembl; ENSMUST00000079176; ENSMUSP00000078175; ENSMUSG00000030701. [Q9QYE9-1]
DR Ensembl; ENSMUST00000107044; ENSMUSP00000102659; ENSMUSG00000030701. [Q9QYE9-4]
DR Ensembl; ENSMUST00000107045; ENSMUSP00000102660; ENSMUSG00000030701. [Q9QYE9-3]
DR Ensembl; ENSMUST00000107046; ENSMUSP00000102661; ENSMUSG00000030701. [Q9QYE9-4]
DR Ensembl; ENSMUST00000107047; ENSMUSP00000102662; ENSMUSG00000030701. [Q9QYE9-2]
DR Ensembl; ENSMUST00000116287; ENSMUSP00000111991; ENSMUSG00000030701. [Q9QYE9-3]
DR GeneID; 27276; -.
DR KEGG; mmu:27276; -.
DR UCSC; uc009ink.2; mouse. [Q9QYE9-1]
DR UCSC; uc009ino.2; mouse. [Q9QYE9-2]
DR CTD; 58473; -.
DR MGI; MGI:1351469; Plekhb1.
DR VEuPathDB; HostDB:ENSMUSG00000030701; -.
DR eggNOG; ENOG502RQ6P; Eukaryota.
DR GeneTree; ENSGT00390000013989; -.
DR HOGENOM; CLU_102020_0_0_1; -.
DR InParanoid; Q9QYE9; -.
DR OMA; HFNVRDV; -.
DR OrthoDB; 1558185at2759; -.
DR PhylomeDB; Q9QYE9; -.
DR TreeFam; TF331787; -.
DR BioGRID-ORCS; 27276; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Plekhb1; mouse.
DR EvolutionaryTrace; Q9QYE9; -.
DR PRO; PR:Q9QYE9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QYE9; protein.
DR Bgee; ENSMUSG00000030701; Expressed in vestibular membrane of cochlear duct and 216 other tissues.
DR ExpressionAtlas; Q9QYE9; baseline and differential.
DR Genevisible; Q9QYE9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; TAS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039816; PLEKHB1.
DR InterPro; IPR039680; PLEKHB1/2.
DR PANTHER; PTHR14309; PTHR14309; 1.
DR PANTHER; PTHR14309:SF7; PTHR14309:SF7; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Membrane; Reference proteome.
FT CHAIN 1..243
FT /note="Pleckstrin homology domain-containing family B
FT member 1"
FT /id="PRO_0000053887"
FT DOMAIN 21..128
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585447,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009781"
FT VAR_SEQ 131..165
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585447,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009782"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2D9V"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2D9V"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2D9V"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2D9V"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2D9V"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2D9V"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:2D9V"
SQ SEQUENCE 243 AA; 27340 MW; 11325285841AF616 CRC64;
MSPATPVPPD SILESPFEEM ALVRGGWLWR QSSILRRWKR NWFALWLDGT LGYYHDETAQ
DEEDRVVIHF NVRDIKVGQE CQDVQPPEGR SRDGLLTVNL REGSRLHLCA ETRDDAIAWK
TALMEANSTP APAGATVPPR SRRVCPKVRC TTLSWNPCKV ERRIWVRVYS PYQDYYEVVP
PNAHEATYVR SYYGPPYAGP GVTHVIVRED PCYSSGAPLA MGMLAGAATG AALGSLMWSP
CWF
