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Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (PH domain-containing protein in retina 1) (PHRET1) (Pleckstrin homology domain retinal protein 1)

 PKHB1_MOUSE             Reviewed;         243 AA.
Q9QYE9; Q9QYB3; Q9QYB4; Q9QYD2; Q9QYD3;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-NOV-2018, entry version 132.
RecName: Full=Pleckstrin homology domain-containing family B member 1;
Short=PH domain-containing family B member 1;
AltName: Full=Evectin-1;
AltName: Full=PH domain-containing protein in retina 1;
Short=PHRET1;
AltName: Full=Pleckstrin homology domain retinal protein 1;
Name=Plekhb1; Synonyms=Evt1, Phr1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
TISSUE SPECIFICITY.
TISSUE=Brain, and Retina;
PubMed=10585447; DOI=10.1074/jbc.274.50.35676;
Xu S., Ladak R., Swanson D.A., Soltyk A., Sun H., Ploder L.,
Vidgen D., Duncan A.M.V., Garami E., McInnes R.R., Valle D.;
"PHR1 encodes an abundant, pleckstrin homology domain-containing
integral membrane protein in the photoreceptor outer segments.";
J. Biol. Chem. 274:35676-35685(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH MYO1C AND MYO7A, AND HOMODIMERIZATION.
PubMed=15976448; DOI=10.1242/jcs.02424;
Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I.,
Pezeron G., Michalski N., Daviet L., Hardelin J.-P., Legrain P.,
Petit C.;
"PHR1, an integral membrane protein of the inner ear sensory cells,
directly interacts with myosin 1c and myosin VIIa.";
J. Cell Sci. 118:2891-2899(2005).
[5]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15456885; DOI=10.1128/MCB.24.20.9137-9151.2004;
Xu S., Wang Y., Zhao H., Zhang L., Xiong W., Yau K.W., Hiel H.,
Glowatzki E., Ryugo D.K., Valle D.;
"PHR1, a PH domain-containing protein expressed in primary sensory
neurons.";
Mol. Cell. Biol. 24:9137-9151(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20301200; DOI=10.1002/lary.20779;
Tan B., Brown D., Xu S., Valle D.;
"PHR1 is a vesicle-bound protein abundantly expressed in mature
olfactory neurons.";
Laryngoscope 120:1002-1010(2010).
[8]
STRUCTURE BY NMR OF 22-138.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PH domain of pleckstrin homology domain-
containing protein family B member 1 from mouse.";
Submitted (JUN-2006) to the PDB data bank.
-!- SUBUNIT: Binds transducins (By similarity). Homodimer. Interacts
(via PH domain) with MYO1C. Interacts (via PH domain) with MYO7A.
{ECO:0000250|UniProtKB:Q9UF11, ECO:0000269|PubMed:15976448}.
-!- INTERACTION:
Q9WTI7:Myo1c; NbExp=4; IntAct=EBI-1127141, EBI-777558;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20301200}.
Cytoplasm {ECO:0000269|PubMed:20301200}. Note=Membrane-associated.
Highly expressed in the outer segments of photoreceptor cells,
both in rods and cones (By similarity). Localizes to the apical
juxta-nuclear Golgi region of the cytoplasm (PubMed:20301200).
{ECO:0000250|UniProtKB:Q9UF11}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9QYE9-1; Sequence=Displayed;
Name=2;
IsoId=Q9QYE9-2; Sequence=VSP_009782;
Name=3;
IsoId=Q9QYE9-3; Sequence=VSP_009781;
Name=4;
IsoId=Q9QYE9-4; Sequence=VSP_009781, VSP_009782;
-!- TISSUE SPECIFICITY: Highly expressed in retina and brain. In
retina, abundantly expressed in photoreceptors. Isoform 4 is the
predominant isoform expressed in mature olfactory receptor neurons
and vestibular and cochlear hair cells. Also expressed in cells
with possible sensory function, including peripheral retinal
ganglion cells, cochlear interdental cells, and neurons of the
circumventricular organ (at protein level).
{ECO:0000269|PubMed:10585447, ECO:0000269|PubMed:15456885,
ECO:0000269|PubMed:20301200}.
-!- DISRUPTION PHENOTYPE: Mice appear normal at birth with no obvious
behavioral or growth abnormalities nor overt sensory deficits. At
6 months and 1 year of age, mice display normal retinal histology
and normal response in electroretinograms.
{ECO:0000269|PubMed:15456885}.
-----------------------------------------------------------------------
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EMBL; AF071000; AAD32952.1; -; mRNA.
EMBL; AF000272; AAF16676.1; -; mRNA.
EMBL; AF071001; AAF16683.1; ALT_TERM; Genomic_DNA.
EMBL; AF101053; AAF18571.1; -; mRNA.
EMBL; AF100613; AAF18933.1; -; mRNA.
EMBL; AK005102; BAB23819.1; -; mRNA.
EMBL; BC024756; AAH24756.1; -; mRNA.
CCDS; CCDS21504.1; -. [Q9QYE9-1]
CCDS; CCDS52324.1; -. [Q9QYE9-4]
CCDS; CCDS52325.1; -. [Q9QYE9-3]
CCDS; CCDS52326.1; -. [Q9QYE9-2]
RefSeq; NP_001156654.1; NM_001163182.1. [Q9QYE9-2]
RefSeq; NP_001156655.1; NM_001163183.1. [Q9QYE9-3]
RefSeq; NP_001156656.1; NM_001163184.1. [Q9QYE9-4]
RefSeq; NP_001156657.1; NM_001163185.1. [Q9QYE9-4]
RefSeq; NP_001156658.1; NM_001163186.1. [Q9QYE9-3]
RefSeq; NP_001156659.1; NM_001163187.1. [Q9QYE9-4]
RefSeq; NP_001278265.1; NM_001291336.1.
RefSeq; NP_038774.1; NM_013746.3. [Q9QYE9-1]
RefSeq; XP_006507969.1; XM_006507906.1. [Q9QYE9-3]
UniGene; Mm.491216; -.
PDB; 2D9V; NMR; -; A=22-138.
PDBsum; 2D9V; -.
ProteinModelPortal; Q9QYE9; -.
SMR; Q9QYE9; -.
BioGrid; 205156; 6.
IntAct; Q9QYE9; 2.
MINT; Q9QYE9; -.
STRING; 10090.ENSMUSP00000078175; -.
iPTMnet; Q9QYE9; -.
PhosphoSitePlus; Q9QYE9; -.
PaxDb; Q9QYE9; -.
PRIDE; Q9QYE9; -.
DNASU; 27276; -.
Ensembl; ENSMUST00000079176; ENSMUSP00000078175; ENSMUSG00000030701. [Q9QYE9-1]
Ensembl; ENSMUST00000107044; ENSMUSP00000102659; ENSMUSG00000030701. [Q9QYE9-4]
Ensembl; ENSMUST00000107045; ENSMUSP00000102660; ENSMUSG00000030701. [Q9QYE9-3]
Ensembl; ENSMUST00000107046; ENSMUSP00000102661; ENSMUSG00000030701. [Q9QYE9-4]
Ensembl; ENSMUST00000107047; ENSMUSP00000102662; ENSMUSG00000030701. [Q9QYE9-2]
Ensembl; ENSMUST00000116287; ENSMUSP00000111991; ENSMUSG00000030701. [Q9QYE9-3]
GeneID; 27276; -.
KEGG; mmu:27276; -.
UCSC; uc009ink.2; mouse. [Q9QYE9-1]
UCSC; uc009ino.2; mouse. [Q9QYE9-2]
CTD; 58473; -.
MGI; MGI:1351469; Plekhb1.
eggNOG; ENOG410IXBE; Eukaryota.
eggNOG; ENOG410Y287; LUCA.
GeneTree; ENSGT00390000013989; -.
HOGENOM; HOG000253945; -.
HOVERGEN; HBG060487; -.
InParanoid; Q9QYE9; -.
OMA; YDPYDDS; -.
OrthoDB; EOG091G14FB; -.
PhylomeDB; Q9QYE9; -.
TreeFam; TF331787; -.
ChiTaRS; Plekhb1; mouse.
EvolutionaryTrace; Q9QYE9; -.
PRO; PR:Q9QYE9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030701; Expressed in 222 organ(s), highest expression level in vestibular membrane of cochlear duct.
ExpressionAtlas; Q9QYE9; baseline and differential.
Genevisible; Q9QYE9; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0001750; C:photoreceptor outer segment; TAS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR039816; PLEKHB1.
InterPro; IPR039680; PLEKHB1/2.
PANTHER; PTHR14309; PTHR14309; 1.
PANTHER; PTHR14309:SF7; PTHR14309:SF7; 1.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; Membrane; Reference proteome.
CHAIN 1 243 Pleckstrin homology domain-containing
family B member 1.
/FTId=PRO_0000053887.
DOMAIN 21 128 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
VAR_SEQ 1 19 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10585447,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009781.
VAR_SEQ 131 165 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:10585447,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009782.
STRAND 22 31 {ECO:0000244|PDB:2D9V}.
STRAND 33 35 {ECO:0000244|PDB:2D9V}.
STRAND 38 46 {ECO:0000244|PDB:2D9V}.
TURN 47 49 {ECO:0000244|PDB:2D9V}.
STRAND 50 58 {ECO:0000244|PDB:2D9V}.
STRAND 60 67 {ECO:0000244|PDB:2D9V}.
TURN 69 71 {ECO:0000244|PDB:2D9V}.
STRAND 72 77 {ECO:0000244|PDB:2D9V}.
HELIX 78 80 {ECO:0000244|PDB:2D9V}.
TURN 92 94 {ECO:0000244|PDB:2D9V}.
STRAND 95 100 {ECO:0000244|PDB:2D9V}.
STRAND 105 109 {ECO:0000244|PDB:2D9V}.
HELIX 113 127 {ECO:0000244|PDB:2D9V}.
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


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