PACS2_MOUSE
ID PACS2_MOUSE Reviewed; 862 AA.
AC Q3V3Q7; E9QKL3; Q80TW2; Q80VG3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphofurin acidic cluster sorting protein 2;
DE Short=PACS-2;
DE AltName: Full=PACS1-like protein;
GN Name=Pacs2; Synonyms=Kiaa0602, Pacs1l;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone;
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 MRNA] OF 56-862.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-862.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-662 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Pancreas;
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).
CC -!- FUNCTION: Multifunctional sorting protein that controls the endoplasmic
CC reticulum (ER)-mitochondria communication, including the apposition of
CC mitochondria with the ER and ER homeostasis. In addition, in response
CC to apoptotic inducer, translocates BIB to mitochondria, which initiates
CC a sequence of events including the formation of mitochondrial truncated
CC BID, the release of cytochrome c, the activation of caspase-3 thereby
CC causing cell death. May also involved in ion channel trafficking,
CC directing acidic cluster-containing ion channels to distinct
CC subcellular compartments (By similarity).
CC {ECO:0000250|UniProtKB:Q86VP3}.
CC -!- SUBUNIT: Interacts with BID and PKD2. Interacts with SIRT1. Interacts
CC with HDAC1. Interacts with TRPV1. {ECO:0000250|UniProtKB:Q86VP3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q86VP3}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q86VP3}.
CC -!- SIMILARITY: Belongs to the PACS family. {ECO:0000305}.
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DR EMBL; AK036581; BAE20504.1; -; mRNA.
DR EMBL; AC073562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122326; BAC65608.1; -; mRNA.
DR EMBL; BC043302; AAH43302.1; -; mRNA.
DR CCDS; CCDS88412.1; -.
DR RefSeq; NP_001278374.1; NM_001291445.1.
DR AlphaFoldDB; Q3V3Q7; -.
DR BioGRID; 229978; 3.
DR STRING; 10090.ENSMUSP00000081953; -.
DR iPTMnet; Q3V3Q7; -.
DR PhosphoSitePlus; Q3V3Q7; -.
DR EPD; Q3V3Q7; -.
DR jPOST; Q3V3Q7; -.
DR MaxQB; Q3V3Q7; -.
DR PaxDb; Q3V3Q7; -.
DR PeptideAtlas; Q3V3Q7; -.
DR PRIDE; Q3V3Q7; -.
DR ProteomicsDB; 287764; -.
DR Antibodypedia; 93; 121 antibodies from 24 providers.
DR Ensembl; ENSMUST00000220541; ENSMUSP00000152145; ENSMUSG00000021143.
DR GeneID; 217893; -.
DR KEGG; mmu:217893; -.
DR UCSC; uc007pfq.2; mouse.
DR CTD; 23241; -.
DR MGI; MGI:1924399; Pacs2.
DR VEuPathDB; HostDB:ENSMUSG00000021143; -.
DR eggNOG; KOG3709; Eukaryota.
DR GeneTree; ENSGT00950000183209; -.
DR InParanoid; Q3V3Q7; -.
DR OrthoDB; 291515at2759; -.
DR BioGRID-ORCS; 217893; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Pacs2; mouse.
DR PRO; PR:Q3V3Q7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q3V3Q7; protein.
DR Bgee; ENSMUSG00000021143; Expressed in gastrula and 238 other tissues.
DR ExpressionAtlas; Q3V3Q7; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:MGI.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISO:MGI.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR InterPro; IPR019381; Phosphofurin_acidic_CS-1.
DR PANTHER; PTHR13280; PTHR13280; 2.
DR Pfam; PF10254; Pacs-1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..862
FT /note="Phosphofurin acidic cluster sorting protein 2"
FT /id="PRO_0000259512"
FT REGION 151..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP3"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP3"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 56..68
FT /note="EKELLSVVIAVKM -> GQVETDLALTFSL (in Ref. 3;
FT BAC65608)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="V -> L (in Ref. 1; BAE20504)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> S (in Ref. 1; BAE20504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 862 AA; 94932 MW; C3702C5537A03B38 CRC64;
MAERGRLGLP GAPGALNTPV PMNLFATWEV DGSSPSCVPR LCSLTLKKLA VLRELEKELL
SVVIAVKMQY PHFLKREGNK LQIMLQRRKR YKNRTILGYK TLAAGSINMA EVMQHPSEGG
QVLSLCSSIK EASVKVAEIW IVSLSSQPID HEDSAMQAGP KTKSTDNYSE EEYESFSSEQ
EASDDAVQGQ DLDEDDFDVG KPKKQRRSIV RTTSMTRQQN FKQKVVALLR RFKVSEEVLD
SEQDPAEHVP EVEEDLDLLY DTLDVENPSD SGPDMDDDDS VLSTPKPKLR PYFEGLSHSS
SQTEIGSIHS ARSHREPPSP ADVPEKTRSL GGKQQLSDSV SDTVALSAAV PREPSGQPED
SPEAETSTLD VFTEKLPPSG RIIKTESLVI PSTRSESKPA GRRGRSTSLK ERQPARPQNE
RANSLDNERC PDTRSQLQIP RKTVYDQLNH ILISDDQLPE NIILVNTSDW QGQFLSDVLQ
KHTLPVVCTC SAADVQAAFS TIVSRIQRYC NCNSQPPTPV KIAVAGAQHY LSAILRLFVE
QLSHKTPDWL GYMRFLIIPL GSHPVARYLG SVDYRYNNFF QDLAWRDLFN KLEAQSSVQD
TPDIVSRITQ YISGANCAHQ LPIAEAMLTY KQKSPDEESS QRFIPFVGVV KVGIVEPSSA
TSGDSDDAAP SSSSILSSTP PSASTSPAAK EASPTPPSSP SVSGGLSSPS QGVGAELMGL
QVDYWTAAQP ADRKRDAEKK DMPTTKNTLK CTFRSLQVSR LPSSGEAAAT PTMSMTVVTK
EKNKKVMFLP KKTKDKEVES KSQCIEGISR LICTAKHQQN MLRVLIDGVE CSDVKFFQLA
AQWSSHVKHF PICIFGHSKA TF
