PALM3_HUMAN
ID PALM3_HUMAN Reviewed; 673 AA.
AC A6NDB9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Paralemmin-3;
DE Flags: Precursor;
GN Name=PALM3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [3]
RP FUNCTION, INTERACTION WITH SIGIRR, AND INDUCTION.
RX PubMed=21187075; DOI=10.1016/j.bbrc.2010.12.104;
RA Chen X., Wu X., Zhao Y., Wang G., Feng J., Li Q., Qian G.;
RT "A novel binding protein of single immunoglobulin IL-1 receptor-related
RT molecule: Paralemmin-3.";
RL Biochem. Biophys. Res. Commun. 404:1029-1033(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-301 AND SER-375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; SER-375 AND SER-420, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-143; THR-151;
RP SER-155; SER-157; SER-260; SER-325; SER-375; SER-420; SER-544 AND SER-660,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-
CC like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}.
CC -!- SUBUNIT: Interacts with SIGIRR. {ECO:0000269|PubMed:21187075}.
CC -!- INTERACTION:
CC A6NDB9; Q6IA17: SIGIRR; NbExp=4; IntAct=EBI-6873185, EBI-719672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS).
CC {ECO:0000269|PubMed:21187075}.
CC -!- PTM: Palmitoylated on Cys-667 and Cys-669 and prenylated on Cys-670;
CC which is required for membrane association. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001138500.1; NM_001145028.1.
DR AlphaFoldDB; A6NDB9; -.
DR SMR; A6NDB9; -.
DR BioGRID; 131220; 11.
DR IntAct; A6NDB9; 10.
DR MINT; A6NDB9; -.
DR STRING; 9606.ENSP00000344996; -.
DR iPTMnet; A6NDB9; -.
DR PhosphoSitePlus; A6NDB9; -.
DR BioMuta; PALM3; -.
DR EPD; A6NDB9; -.
DR jPOST; A6NDB9; -.
DR MassIVE; A6NDB9; -.
DR MaxQB; A6NDB9; -.
DR PaxDb; A6NDB9; -.
DR PeptideAtlas; A6NDB9; -.
DR PRIDE; A6NDB9; -.
DR ProteomicsDB; 898; -.
DR Antibodypedia; 57000; 97 antibodies from 21 providers.
DR DNASU; 342979; -.
DR Ensembl; ENST00000340790.9; ENSP00000344996.3; ENSG00000187867.10.
DR Ensembl; ENST00000672551.1; ENSP00000500424.1; ENSG00000288318.1.
DR GeneID; 342979; -.
DR KEGG; hsa:342979; -.
DR UCSC; uc010xnk.2; human.
DR CTD; 342979; -.
DR GeneCards; PALM3; -.
DR HGNC; HGNC:33274; PALM3.
DR HPA; ENSG00000187867; Tissue enhanced (kidney, liver, pancreas, stomach).
DR neXtProt; NX_A6NDB9; -.
DR OpenTargets; ENSG00000187867; -.
DR PharmGKB; PA165393890; -.
DR VEuPathDB; HostDB:ENSG00000187867; -.
DR eggNOG; ENOG502S32R; Eukaryota.
DR GeneTree; ENSGT00390000009016; -.
DR HOGENOM; CLU_401664_0_0_1; -.
DR InParanoid; A6NDB9; -.
DR OMA; ALQSQVW; -.
DR OrthoDB; 979127at2759; -.
DR PhylomeDB; A6NDB9; -.
DR TreeFam; TF337206; -.
DR PathwayCommons; A6NDB9; -.
DR SignaLink; A6NDB9; -.
DR BioGRID-ORCS; 342979; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; PALM3; human.
DR GenomeRNAi; 342979; -.
DR Pharos; A6NDB9; Tbio.
DR PRO; PR:A6NDB9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A6NDB9; protein.
DR Bgee; ENSG00000187867; Expressed in metanephros cortex and 89 other tissues.
DR ExpressionAtlas; A6NDB9; baseline and differential.
DR Genevisible; A6NDB9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:UniProtKB.
DR InterPro; IPR004965; Paralemmin.
DR InterPro; IPR024149; Paralemmin-3.
DR PANTHER; PTHR47528; PTHR47528; 1.
DR Pfam; PF03285; Paralemmin; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Cytoplasm; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat.
FT CHAIN 1..670
FT /note="Paralemmin-3"
FT /id="PRO_0000332171"
FT PROPEP 671..673
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000332172"
FT REGION 49..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..49
FT /evidence="ECO:0000255"
FT COILED 75..101
FT /evidence="ECO:0000255"
FT COMPBIAS 387..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 670
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 667
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 669
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 670
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 440
FT /note="A -> T (in dbSNP:rs11880169)"
FT /id="VAR_053804"
SQ SEQUENCE 673 AA; 71695 MW; 70D97AAD9418E6A2 CRC64;
MAESSLYRQR LEVIAEKRRL QEEIRAARRE VEEEKLRVER LKRKSLRERW LMDGAAAVPE
PSEDPTSKDP QSPEGQAQAR IRNLEDSLFT LQSQLQLLQS ASTGAQHKPS GRPSWRRQGH
RPLSQSIVEA GSVGQTDLNK RASLPAGLVG TPPESPSEPR EDVLGFLPGP RQVPGAAGDS
SEANGPCPSP IPTPEQGLSQ RAVPSEGRVG EAKGGGVVSV VWEGLRATED CATGATGPEL
EAKVEEVVLE AIGDRKGAGS LELPAWVKED RGIVEVVWEG VGGSDAEAMG EIGRVPEVVQ
TSSPRLQERL EAAASIEGED VPQGSPEGDG QGGSGGEEGS FIWVERVTLS EEWEELLVEG
LEGPEVAGRE RGDESPLGAE GAKTGGGEET WEAEKRKAEE SMGIGSEEKP GTGRDEAEMS
PVVERKGGEK KLELESRGSA EKLGTEREGG EEPLGIERKV EGHLRAEKEG DEEKRGAEEE
EVEEPLGVEK KGGEEEPEAT KEPLEAERKG GEETLEAEKR GGEESLETEK TQGTEGDLNL
EQGSREGSES QAEEMNEAGP PLEANTETRP EKEGPQPQEK PVGALEEEGV KPQTAAEGQG
PLGDATPLLA ETPAPEQPAE CQPLLQGEGP SANPSAHPVP TYAPARQPEP SAPTEGEEAS
GPKQKTCQCC AVM
