PKHN1_MOUSE
ID PKHN1_MOUSE Reviewed; 610 AA.
AC Q8C886; A0A1W2P6Q7; A0A1W2P7X5; Q8R3H1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable pleckstrin homology domain-containing family N member 1;
DE Short=PH domain-containing family N member 1;
DE AltName: Full=Cardiolipin and phosphatidic acid-binding protein {ECO:0000303|PubMed:27616329};
GN Name=Plekhn1; Synonyms=Clpabp {ECO:0000303|PubMed:27616329};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 360-598 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Retina;
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27616329; DOI=10.1016/j.bbalip.2016.09.006;
RA Nishino T., Matsunaga R., Jikihara H., Uchida M., Maeda A., Qi G., Abe T.,
RA Kiyonari H., Tashiro S., Inagaki-Ohara K., Shimamoto F., Konishi H.;
RT "Antagonizing effect of CLPABP on the function of HuR as a regulator of
RT ARE-containing leptin mRNA stability and the effect of its depletion on
RT obesity in old male mouse.";
RL Biochim. Biophys. Acta 1861:1816-1827(2016).
CC -!- FUNCTION: Controls the stability of the leptin mRNA harboring an AU-
CC rich element (ARE) in its 3' UTR, in cooperation with the RNA
CC stabilizer ELAVL1. Decreases the stability of the leptin mRNA by
CC antagonizing the function of ELAVL1 by inducing its atypical
CC recruitment from the nucleus to the cytosol (PubMed:27616329). Binds to
CC cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-
CC phosphate (PtdIns(4)P) and phosphatidylserine (PS) (By similarity).
CC {ECO:0000250|UniProtKB:Q494U1, ECO:0000269|PubMed:27616329}.
CC -!- SUBUNIT: Found in a complex with cytochrome c mRNA and various
CC ribosomal proteins. Interacts with C1QBP, ELAVL1 and BID.
CC {ECO:0000250|UniProtKB:Q494U1}.
CC -!- INTERACTION:
CC Q8C886; P39428: Traf1; NbExp=6; IntAct=EBI-646708, EBI-520123;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q494U1};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion
CC {ECO:0000269|PubMed:27616329}. Note=Interaction with C1QBP and
CC phosphorylation is essential for its mitochondrial localization.
CC Localizes on the microtubule in the form of small granules.
CC {ECO:0000250|UniProtKB:Q494U1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C886-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C886-2; Sequence=VSP_059841, VSP_059842, VSP_059843;
CC Name=3;
CC IsoId=Q8C886-3; Sequence=VSP_059844, VSP_059845;
CC -!- TISSUE SPECIFICITY: Testis and adipose tissue (at protein level).
CC Ubiquitous. {ECO:0000269|PubMed:27616329}.
CC -!- DOMAIN: Both PH domains are essential for its mitochondrial
CC localization. {ECO:0000250|UniProtKB:Q494U1}.
CC -!- PTM: Phosphorylation is essential for its mitochondrial localization
CC and regulates its interaction with C1QBP.
CC {ECO:0000250|UniProtKB:Q494U1}.
CC -!- DISRUPTION PHENOTYPE: Male knockout mice (KO) gradually become fat
CC after 20 weeks of age compared to the wild-type (WT) mice. At 36 weeks,
CC weight differences in whole body, epididymal fat pad, and liver between
CC the KO and WT mice is significant. KO mice exhibit a hyperphagia
CC phenotype with the plasma concentration of leptin higher in the KO mice
CC than in the WT mice. {ECO:0000269|PubMed:27616329}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK048084; BAC33236.1; -; mRNA.
DR EMBL; CAAA01066806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01066807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15087.1; -; Genomic_DNA.
DR EMBL; CH466594; EDL15088.1; -; Genomic_DNA.
DR EMBL; BC031374; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC025458; AAH25458.1; -; mRNA.
DR CCDS; CCDS89875.1; -. [Q8C886-1]
DR AlphaFoldDB; Q8C886; -.
DR SMR; Q8C886; -.
DR IntAct; Q8C886; 2.
DR STRING; 10090.ENSMUSP00000101196; -.
DR iPTMnet; Q8C886; -.
DR PhosphoSitePlus; Q8C886; -.
DR MaxQB; Q8C886; -.
DR PaxDb; Q8C886; -.
DR PRIDE; Q8C886; -.
DR ProteomicsDB; 289915; -. [Q8C886-1]
DR ProteomicsDB; 289916; -. [Q8C886-2]
DR ProteomicsDB; 332938; -.
DR ProteomicsDB; 339243; -.
DR Antibodypedia; 26039; 19 antibodies from 11 providers.
DR Ensembl; ENSMUST00000217885; ENSMUSP00000151799; ENSMUSG00000078485. [Q8C886-1]
DR Ensembl; ENSMUST00000218699; ENSMUSP00000151311; ENSMUSG00000078485. [Q8C886-3]
DR MGI; MGI:2387630; Plekhn1.
DR VEuPathDB; HostDB:ENSMUSG00000078485; -.
DR eggNOG; ENOG502QSRE; Eukaryota.
DR GeneTree; ENSGT00390000003618; -.
DR InParanoid; Q8C886; -.
DR PhylomeDB; Q8C886; -.
DR ChiTaRS; Plekhn1; mouse.
DR PRO; PR:Q8C886; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8C886; protein.
DR Bgee; ENSMUSG00000078485; Expressed in lip and 125 other tissues.
DR ExpressionAtlas; Q8C886; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR042835; PLEKHN1.
DR PANTHER; PTHR46882; PTHR46882; 1.
DR SMART; SM00233; PH; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Lipoprotein; Membrane; Mitochondrion;
KW Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q494U1"
FT CHAIN 2..610
FT /note="Probable pleckstrin homology domain-containing
FT family N member 1"
FT /id="PRO_0000309364"
FT DOMAIN 96..192
FT /note="PH 1"
FT DOMAIN 227..324
FT /note="PH 2"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..100
FT /note="Interaction with C1QBP"
FT /evidence="ECO:0000250|UniProtKB:Q494U1"
FT REGION 327..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q494U1"
FT MOD_RES 462
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q494U1"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q494U1"
FT VAR_SEQ 1..188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_059841"
FT VAR_SEQ 485..547
FT /note="FLCAIQTSPGPDLSSPFPPVSVSVPVSESSSGISSSPGPLGSHLLTKKGALQ
FT PRASQRHRGSF -> LWHLQLAWASGLPLTHQERCPATQSFPETPGFLQEQRPTALRLP
FT SACHPCQRRQTQFPAPSPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_059842"
FT VAR_SEQ 548..610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_059843"
FT VAR_SEQ 561..571
FT /note="VTPAREGKPSS -> GRGCYFSKAGA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059844"
FT VAR_SEQ 572..610
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059845"
FT CONFLICT 360..362
FT /note="WKL -> TRP (in Ref. 4; AAH25458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 66826 MW; 1FC9CC3ADD12F475 CRC64;
MGNSHCVPQA PRRLRASFSR KPSLKGNRED SARKLAGLFG TEARPDGDTA ANRIFHYIPG
TDIPGPEHHP ENLEQPFLSV FKKGWRRTPV RNLGKVVHYS KVRLRFQHSQ DISDCYLELF
PSHLYFQAHG SEGLTFQGLL PLTELNICPT DGSREHAFQI TGPLPAPLLV LCHSEAELSH
WLYHLEKQMA LLGLQRCHSA PPQGSLGDKP PWTQLRRAYG CGSMSGAICA SRVKLQHLPS
QEQWDRLLVL YPASLAIFSE EPEGLSFKGE LPLSAIHINL EEKEKEIRSF LIEGHLINTI
RVVCASYEDY SQWLLCLRTV SRRDGAHLPP GPESFPGLQK PTQLVGRGRG SLSSNGRSSW
KLECPVFPTS QSLPESSVPT TIGFPAPPVP NQTDSNCVST GQKKMKPSDS SPSPRGRAQR
EVSGSTVPLP LPLDLTKMSA LNLDSGPEAQ DHSLDIPHSP LYADPYTPPA TSRHKITDIQ
GLDEFLCAIQ TSPGPDLSSP FPPVSVSVPV SESSSGISSS PGPLGSHLLT KKGALQPRAS
QRHRGSFKSR GPQPSDFPQL VTPAREGKPS SLPPPPDEEA PIWNKTSSPS HPKWPQPRKP
AVEGGFIQWI
