PACS1_RAT
ID PACS1_RAT Reviewed; 961 AA.
AC O88588; O88589;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phosphofurin acidic cluster sorting protein 1;
DE Short=PACS-1;
GN Name=Pacs1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PACS-1A AND PACS-1B), SUBUNIT,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-379; SER-526 AND
RP SER-527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000269|PubMed:9695949}.
CC -!- SUBUNIT: Associates with AP-1 and AP-3 but not with AP-2 complexes (By
CC similarity). Interacts with FURIN (By similarity). Forms a ternary
CC complex with furin and AP-1 (PubMed:9695949). Interacts with PKD2 (via
CC acidic region) (By similarity). Interacts with SORL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6VY07, ECO:0000250|UniProtKB:Q8K212}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:9695949}. Note=Localizes in the perinuclear region,
CC probably the TGN. {ECO:0000269|PubMed:9695949}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PACS-1a;
CC IsoId=O88588-1; Sequence=Displayed;
CC Name=PACS-1b;
CC IsoId=O88588-2; Sequence=VSP_011558, VSP_011559;
CC -!- SIMILARITY: Belongs to the PACS family. {ECO:0000305}.
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DR EMBL; AF076183; AAC31815.1; -; mRNA.
DR EMBL; AF076184; AAC31816.1; -; mRNA.
DR RefSeq; NP_599233.1; NM_134406.1. [O88588-1]
DR AlphaFoldDB; O88588; -.
DR BioGRID; 251254; 1.
DR IntAct; O88588; 1.
DR MINT; O88588; -.
DR STRING; 10116.ENSRNOP00000027632; -.
DR iPTMnet; O88588; -.
DR PhosphoSitePlus; O88588; -.
DR SwissPalm; O88588; -.
DR jPOST; O88588; -.
DR PaxDb; O88588; -.
DR PRIDE; O88588; -.
DR Ensembl; ENSRNOT00000027632; ENSRNOP00000027632; ENSRNOG00000020350. [O88588-1]
DR GeneID; 171444; -.
DR KEGG; rno:171444; -.
DR UCSC; RGD:620579; rat. [O88588-1]
DR CTD; 55690; -.
DR RGD; 620579; Pacs1.
DR eggNOG; KOG3709; Eukaryota.
DR GeneTree; ENSGT00950000183209; -.
DR InParanoid; O88588; -.
DR PhylomeDB; O88588; -.
DR PRO; PR:O88588; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:RGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
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; Alternative splicing; Coiled coil; Golgi apparatus;
KW Phosphoprotein; 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_0000058173"
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 45..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:0000250|UniProtKB:Q8K212"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K212"
FT MOD_RES 249
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8K212"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
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:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VY07"
FT VAR_SEQ 541..559
FT /note="IPRKVVYDQLNQILVSDAA -> VILGSSRFRTPFLDFSLFL (in
FT isoform PACS-1b)"
FT /evidence="ECO:0000303|PubMed:9695949"
FT /id="VSP_011558"
FT VAR_SEQ 560..961
FT /note="Missing (in isoform PACS-1b)"
FT /evidence="ECO:0000303|PubMed:9695949"
FT /id="VSP_011559"
SQ SEQUENCE 961 AA; 104700 MW; 9B4A4522DFF9DEAF CRC64;
MAERGGAGGG PGGAGGGSSQ RGSGVAQSPQ QQPPQQPSQP 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 QDMFGDASTS LVVPEKVKTP
MKSSKADLQG SASPSKVEGT HTPRQKRSTP LKERQLSKPL SERTNSSDSE RSPDLGHSTQ
IPRKVVYDQL NQILVSDAAL PENVILVNTT DWQGQYVAEL LQDQRKPVVC TCSTVEVQAV
LSALLTRIQR YCNCNSSMPR PVKVAAVGSQ SYLSSILRFF VKSLASKTPD WLGHMRFLIV
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 PVGLFSGSKP
T
