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   27-MAR-2024, entry version 110.
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. Interacts with WDR37.
CC       {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   GlyGen; Q3V3Q7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3V3Q7; -.
DR   PhosphoSitePlus; Q3V3Q7; -.
DR   EPD; Q3V3Q7; -.
DR   jPOST; Q3V3Q7; -.
DR   MaxQB; Q3V3Q7; -.
DR   PaxDb; 10090-ENSMUSP00000081953; -.
DR   PeptideAtlas; Q3V3Q7; -.
DR   ProteomicsDB; 287764; -.
DR   Pumba; Q3V3Q7; -.
DR   Antibodypedia; 93; 126 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000220541.2; ENSMUSP00000152145.2; ENSMUSG00000021143.11.
DR   GeneID; 217893; -.
DR   KEGG; mmu:217893; -.
DR   UCSC; uc007pfq.2; mouse.
DR   AGR; MGI:1924399; -.
DR   CTD; 23241; -.
DR   MGI; MGI:1924399; Pacs2.
DR   VEuPathDB; HostDB:ENSMUSG00000021143; -.
DR   eggNOG; KOG3709; Eukaryota.
DR   GeneTree; ENSGT00950000183209; -.
DR   InParanoid; Q3V3Q7; -.
DR   OrthoDB; 2878701at2759; -.
DR   BioGRID-ORCS; 217893; 0 hits in 80 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 241 other cell types or 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; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN; 1.
DR   PANTHER; PTHR13280:SF15; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 2; 1.
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
//