PACS1_MOUSE
ID PACS1_MOUSE Reviewed; 961 AA.
AC Q8K212; Q6P5H8;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphofurin acidic cluster sorting protein 1;
DE Short=PACS-1;
GN Name=Pacs1;
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=Brain, and 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 [2]
RP INTERACTION WITH FURIN.
RX PubMed=9695949; DOI=10.1016/s0092-8674(00)81420-8;
RA Wan L., Molloy S.S., Thomas L., Liu G., Xiang Y., Rybak S.L., Thomas G.;
RT "PACS-1 defines a novel gene family of cytosolic sorting proteins required
RT for trans-Golgi network localization.";
RL Cell 94:205-216(1998).
RN [3]
RP INTERACTION WITH PKD2.
RX PubMed=15692563; DOI=10.1038/sj.emboj.7600566;
RA Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B.,
RA Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K.,
RA Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.;
RT "Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion
RT channel regulation.";
RL EMBO J. 24:705-716(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-44; TYR-249; SER-428;
RP SER-529 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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: Coat protein that is involved in the localization of trans-
CC Golgi network (TGN) membrane proteins that contain acidic cluster
CC sorting motifs. Controls the endosome-to-Golgi trafficking of furin and
CC mannose-6-phosphate receptor by connecting the acidic-cluster-
CC containing cytoplasmic domain of these molecules with the adapter-
CC protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits (By
CC similarity). {ECO:0000250|UniProtKB:O88588,
CC ECO:0000250|UniProtKB:Q6VY07}.
CC -!- SUBUNIT: Associates with AP-1 and AP-3 but not with AP-2 complexes (By
CC similarity). Interacts with FURIN (PubMed:9695949). Forms a ternary
CC complex with FURIN and AP-1 (By similarity). Interacts with PKD2 (via
CC acidic region) (PubMed:15692563). Interacts with SORL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6VY07, ECO:0000269|PubMed:15692563,
CC ECO:0000269|PubMed:9695949}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:O88588}. Note=Localizes in the perinuclear
CC region, probably the TGN. {ECO:0000250|UniProtKB:O88588}.
CC -!- SIMILARITY: Belongs to the PACS family. {ECO:0000305}.
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DR EMBL; BC062886; AAH62886.1; -; mRNA.
DR EMBL; BC034670; AAH34670.1; -; mRNA.
DR CCDS; CCDS29453.1; -.
DR RefSeq; NP_694769.2; NM_153129.2.
DR AlphaFoldDB; Q8K212; -.
DR BioGRID; 223732; 14.
DR IntAct; Q8K212; 2.
DR MINT; Q8K212; -.
DR STRING; 10090.ENSMUSP00000025786; -.
DR iPTMnet; Q8K212; -.
DR PhosphoSitePlus; Q8K212; -.
DR SwissPalm; Q8K212; -.
DR EPD; Q8K212; -.
DR jPOST; Q8K212; -.
DR MaxQB; Q8K212; -.
DR PaxDb; Q8K212; -.
DR PeptideAtlas; Q8K212; -.
DR PRIDE; Q8K212; -.
DR ProteomicsDB; 287763; -.
DR Antibodypedia; 44366; 97 antibodies from 27 providers.
DR DNASU; 107975; -.
DR Ensembl; ENSMUST00000025786; ENSMUSP00000025786; ENSMUSG00000024855.
DR GeneID; 107975; -.
DR KEGG; mmu:107975; -.
DR UCSC; uc008gci.1; mouse.
DR CTD; 55690; -.
DR MGI; MGI:1277113; Pacs1.
DR VEuPathDB; HostDB:ENSMUSG00000024855; -.
DR eggNOG; KOG3709; Eukaryota.
DR GeneTree; ENSGT00950000183209; -.
DR HOGENOM; CLU_013074_0_0_1; -.
DR InParanoid; Q8K212; -.
DR OMA; LVNATDW; -.
DR OrthoDB; 291515at2759; -.
DR PhylomeDB; Q8K212; -.
DR TreeFam; TF314240; -.
DR BioGRID-ORCS; 107975; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Pacs1; mouse.
DR PRO; PR:Q8K212; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K212; protein.
DR Bgee; ENSMUSG00000024855; Expressed in granulocyte and 244 other tissues.
DR ExpressionAtlas; Q8K212; baseline and differential.
DR Genevisible; Q8K212; MM.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR InterPro; IPR019381; Phosphofurin_acidic_CS-1.
DR PANTHER; PTHR13280; PTHR13280; 1.
DR Pfam; PF10254; Pacs-1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Golgi apparatus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT CHAIN 2..961
FT /note="Phosphofurin acidic cluster sorting protein 1"
FT /id="PRO_0000058172"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..375
FT /evidence="ECO:0000255"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88588"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 816
FT /note="D -> E (in Ref. 1; AAH34670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 104829 MW; A57F3D86800D9B83 CRC64;
MAERGGAGGG PGGSGGGSSQ RGSGVAQSPQ QQPQQQPPQP QQPTPPKLAQ ATSSSSSTSA
AAASSSSSST STSMAVAVAS GSAPPGGPGP GRTPAPVQMN LYATWEVDRS SSSCVPRLFS
LTLKKLVMLK EMDKDLNSVV IAVKLQGSKR ILRSNEIILP ASGLVETELQ LTFSLQYPHF
LKRDANKLQI MLQRRKRYKN RTILGYKTLA VGLINMAEVM QHPNEGALVL GLHSNVKDVS
VPVAEIKIYS LSSQPIDHEG IKSKLSDRSP DIDNYSEEEE ESFSSEQEGS DDPLHGQDLF
YEDEDLRKVK KTRRKLTSTS AITRQPNIKQ KFVALLKRFK VSDEVGFGLE HVSREQIREV
EEDLDELYDS LEMYNPSDSG PEMEETESIL STPKPKLKPF FEGMSQSSSQ TEIGSLNSKG
SLGKDTTSPM ELAALEKVKS TWIKNQDDSL TETDTLEITD QDMFGDVSTS LVVPEKVKTP
MKSSKADLQG SASPSKVEGT HTPRQKRSTP LKERQLSKPL SERTNSSDSE RSPDLGHSTQ
IPRKVVYDQL NQILVSDAAL PENVILVNTT DWQGQYVAEL LQDQRKPVVC TCSTVEVQAV
LSALLTRIQR YCNCNSSMPR PVKVAAVGSQ SYLSSILRFF VKSLASKTPD WLGYMRFLII
PLGSHPVAKY LGSVDSRYSS TFLDSAWRDL FSRSEPPVSE PLDVVGRVMQ YVNGATTTHQ
LPVAEAMLTC RHKFPDEDSY QKFIPFIGVV KVGLVEDSPS TAGDGDDSPV VSLTVPSTSP
PSSSGLSRDA TATPPSSPSM SSALAIVGSP NSPYGDVIGL QVDYWLGHPG ERRREGDKRD
ASSKNTLKSV FRSVQVSRLP HAGEAQLSGT MAMTVVTKEK NKKVPTIFLS KKPREKEVDS
KSQVIEGISR LICSAKQQQT MLRVSIDGVE WSDIKFFQLA AQWPTHVKHF PVGLFSGSKT
T
