PKHB2_MOUSE
ID PKHB2_MOUSE Reviewed; 221 AA.
AC Q9QZC7; Q3UDH6; Q8C4I4; Q8CA27;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Pleckstrin homology domain-containing family B member 2;
DE Short=PH domain-containing family B member 2;
DE AltName: Full=Evectin-2;
GN Name=Plekhb2; Synonyms=Evt2;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10200314; DOI=10.1073/pnas.96.8.4633;
RA Krappa R., Nguyen A., Burrola P., Deretic D., Lemke G.;
RT "Evectins: vesicular proteins that carry a pleckstrin homology domain and
RT localize to post-Golgi membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4633-4638(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Lung, and Spinal cord;
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 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 STRUCTURE BY NMR OF 3-110.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of evectin-2 from mouse.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in retrograde transport of recycling endosomes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250};
CC Peripheral membrane protein. Note=Specifically detected in
CC tubulovesicular structures, and colocalizes with TFNR. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QZC7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZC7-2; Sequence=VSP_009786;
CC Name=3;
CC IsoId=Q9QZC7-3; Sequence=VSP_009785;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, retina, heart and
CC kidney. Detected at lower levels in lung, muscle and nerve.
CC {ECO:0000269|PubMed:10200314}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at birth and up to day 3;
CC expressed at lower levels in embryo and adult.
CC -!- DOMAIN: The PH domain specifically binds phosphatidylserine, which is
CC enriched in recycling endosome membranes, it doesn't recognize PIPs.
CC {ECO:0000250}.
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DR EMBL; AF189817; AAF01332.1; -; mRNA.
DR EMBL; AK039771; BAC30448.1; -; mRNA.
DR EMBL; AK082118; BAC38413.1; -; mRNA.
DR EMBL; AK149868; BAE29136.1; -; mRNA.
DR EMBL; AK150074; BAE29285.1; -; mRNA.
DR EMBL; AK166091; BAE38565.1; -; mRNA.
DR EMBL; BC057994; AAH57994.1; -; mRNA.
DR CCDS; CCDS14874.1; -. [Q9QZC7-1]
DR CCDS; CCDS78558.1; -. [Q9QZC7-3]
DR RefSeq; NP_663491.1; NM_145516.2. [Q9QZC7-1]
DR RefSeq; XP_006495961.1; XM_006495898.3. [Q9QZC7-1]
DR RefSeq; XP_017175721.1; XM_017320232.1.
DR PDB; 2DHI; NMR; -; A=3-109.
DR PDBsum; 2DHI; -.
DR AlphaFoldDB; Q9QZC7; -.
DR SMR; Q9QZC7; -.
DR STRING; 10090.ENSMUSP00000027297; -.
DR iPTMnet; Q9QZC7; -.
DR PhosphoSitePlus; Q9QZC7; -.
DR MaxQB; Q9QZC7; -.
DR PaxDb; Q9QZC7; -.
DR PRIDE; Q9QZC7; -.
DR ProteomicsDB; 289508; -. [Q9QZC7-1]
DR ProteomicsDB; 289509; -. [Q9QZC7-2]
DR ProteomicsDB; 289510; -. [Q9QZC7-3]
DR Antibodypedia; 35075; 74 antibodies from 19 providers.
DR DNASU; 226971; -.
DR Ensembl; ENSMUST00000027297; ENSMUSP00000027297; ENSMUSG00000026123. [Q9QZC7-1]
DR Ensembl; ENSMUST00000156687; ENSMUSP00000140475; ENSMUSG00000026123. [Q9QZC7-3]
DR GeneID; 226971; -.
DR KEGG; mmu:226971; -.
DR UCSC; uc007apl.1; mouse. [Q9QZC7-1]
DR CTD; 55041; -.
DR MGI; MGI:2385825; Plekhb2.
DR VEuPathDB; HostDB:ENSMUSG00000026123; -.
DR eggNOG; ENOG502R270; Eukaryota.
DR GeneTree; ENSGT00390000013989; -.
DR HOGENOM; CLU_102020_0_0_1; -.
DR InParanoid; Q9QZC7; -.
DR OMA; LEDKIHM; -.
DR OrthoDB; 1558185at2759; -.
DR PhylomeDB; Q9QZC7; -.
DR TreeFam; TF331787; -.
DR BioGRID-ORCS; 226971; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Plekhb2; mouse.
DR EvolutionaryTrace; Q9QZC7; -.
DR PRO; PR:Q9QZC7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QZC7; protein.
DR Bgee; ENSMUSG00000026123; Expressed in choroid plexus of fourth ventricle and 245 other tissues.
DR ExpressionAtlas; Q9QZC7; baseline and differential.
DR Genevisible; Q9QZC7; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
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; IPR039680; PLEKHB1/2.
DR InterPro; IPR039815; PLEKHB2.
DR PANTHER; PTHR14309; PTHR14309; 1.
DR PANTHER; PTHR14309:SF8; PTHR14309:SF8; 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; Endosome; Membrane; Reference proteome.
FT CHAIN 1..221
FT /note="Pleckstrin homology domain-containing family B
FT member 2"
FT /id="PRO_0000053890"
FT DOMAIN 2..109
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT BINDING 20
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250"
FT VAR_SEQ 178..221
FT /note="VYGQQPANQVIIRERYRDNDSDLALGMLAGAATGMALGSLFWVF -> NARW
FT LPLPVSAYSGARRRRPPFQLEVK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009785"
FT VAR_SEQ 194..221
FT /note="RDNDSDLALGMLAGAATGMALGSLFWVF -> QDYGVRTL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009786"
FT CONFLICT 81
FT /note="C -> W (in Ref. 2; BAC30448)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> G (in Ref. 2; BAC38413)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2DHI"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2DHI"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2DHI"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2DHI"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2DHI"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:2DHI"
SQ SEQUENCE 221 AA; 24574 MW; 36B1E3CA014E1C66 CRC64;
MAFVKSGWLL RQSTILKRWK KNWFDLWSDG HLIYYDDQTR QSIEDKVHMP VDCINIRTGH
ECRDIQPPDG KPRDCLLQIV CRDGKTISLC AESTDDCLAW KFTLQDSRTN TAYVGSAILS
EETAVAASPP PYAAYATPTP EVYGYGPYSG AYPAGTQVVY AANGQAYAVP YQYPYAGVYG
QQPANQVIIR ERYRDNDSDL ALGMLAGAAT GMALGSLFWV F
