PALM3_MOUSE
ID PALM3_MOUSE Reviewed; 734 AA.
AC A2TJV2; Q9CRS0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Paralemmin-3;
DE Flags: Precursor;
GN Name=Palm3;
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 [MRNA].
RA Hultqvist G., Neumann N.G., Kilimann M.W.;
RT "Characterization of paralemmin-3, a new isoform of the paralemmin protein
RT family implicated in membrane dynamics.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-442.
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
RP IDENTIFICATION.
RX PubMed=11478809; DOI=10.1006/bbrc.2001.5329;
RA Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.;
RT "The paralemmin protein family: identification of paralemmin-2, an isoform
RT differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a more distant
RT cytosolic relative.";
RL Biochem. Biophys. Res. Commun. 285:1369-1376(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-270; SER-332;
RP SER-335; SER-451 AND SER-601, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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: ATP-binding protein, which may act as a adapter in the Toll-
CC like receptor (TLR) signaling. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SIGIRR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- PTM: Palmitoylated on Cys-728 and Cys-730 and prenylated on Cys-731;
CC which is required for membrane association. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29393.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB29393.3; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; EF208034; ABM92364.1; -; mRNA.
DR EMBL; AK014493; BAB29393.3; ALT_SEQ; mRNA.
DR CCDS; CCDS40405.1; -.
DR RefSeq; NP_083153.1; NM_028877.1.
DR AlphaFoldDB; A2TJV2; -.
DR SMR; A2TJV2; -.
DR BioGRID; 216674; 1.
DR STRING; 10090.ENSMUSP00000051396; -.
DR iPTMnet; A2TJV2; -.
DR PhosphoSitePlus; A2TJV2; -.
DR jPOST; A2TJV2; -.
DR MaxQB; A2TJV2; -.
DR PaxDb; A2TJV2; -.
DR PeptideAtlas; A2TJV2; -.
DR PRIDE; A2TJV2; -.
DR ProteomicsDB; 294377; -.
DR Antibodypedia; 57000; 97 antibodies from 21 providers.
DR Ensembl; ENSMUST00000055077; ENSMUSP00000051396; ENSMUSG00000047986.
DR GeneID; 74337; -.
DR KEGG; mmu:74337; -.
DR UCSC; uc009mlq.1; mouse.
DR CTD; 342979; -.
DR MGI; MGI:1921587; Palm3.
DR VEuPathDB; HostDB:ENSMUSG00000047986; -.
DR eggNOG; ENOG502S32R; Eukaryota.
DR GeneTree; ENSGT00390000009016; -.
DR HOGENOM; CLU_401664_0_0_1; -.
DR InParanoid; A2TJV2; -.
DR OMA; ALQSQVW; -.
DR OrthoDB; 979127at2759; -.
DR PhylomeDB; A2TJV2; -.
DR TreeFam; TF337206; -.
DR BioGRID-ORCS; 74337; 2 hits in 71 CRISPR screens.
DR PRO; PR:A2TJV2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; A2TJV2; protein.
DR Bgee; ENSMUSG00000047986; Expressed in yolk sac and 71 other tissues.
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; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0008063; P:Toll signaling pathway; ISO:MGI.
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..731
FT /note="Paralemmin-3"
FT /id="PRO_0000332173"
FT PROPEP 732..734
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000332174"
FT REGION 62..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..64
FT /evidence="ECO:0000255"
FT COILED 90..116
FT /evidence="ECO:0000255"
FT COMPBIAS 62..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NDB9"
FT MOD_RES 731
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 728
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 730
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 731
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 734 AA; 78788 MW; AB071126A771653F CRC64;
MALQTPVLSP ATPTVMAESA LYRQRLEVIA EKRRLQEEIG AARRELEEEK LRVERLKRKS
LRERWLMDGA AEGPERPEEP ASKDPQSPEG QAQARIRNLE DSLFSLQSQL QLLQSASTGA
QHRPAGRPAW RREGPRPLSQ SAMEAAPTAP TDVDKRTSLP DAPVGMSPES PSDPREESIA
VLPASRPSTE AIGTSSEANG PCPGHSPLPE QLSLGVSSVT KAKGDGAVEV VWAGLRATEN
SATGPTDVEL EAKVEEVVLE AIGARQGTSS PELPTWVKEG RGVVEVVWEG LGGRDLDVTG
ESGRDAEATH TSSRRLQEQF EAETCRKEEG ASRDSLEGVG QGGPGVEEGS FIWVERVALS
EDWEEILMEG LEAPQGAGSA GEPEALIGAQ PRGGEASWEV EKREVEKVEG IEEKGRAEKL
GAEREDGVAV LPDETQGREE NEAEKVERKD SEGPFPAEIA TDEEKWEVKT TEGEESLEVE
KGGEAEPVTT EKPLVTEKKP EGSLETERKG SEMPLDQEKD GEGSLDRESK TTEILLDGEI
GDKSSLDETK GSKKLLDEKT GGEGSLDEEA EGSKKLLDRE ADGIEPFSEV DKTSGAKDDV
SPEEQGKANE GAEFQAEDAS PPGATVCVQD EPRSEEQGQQ EPEKQEGLVE GAASKPEPCT
EREGPPGDAT LLLAETPAPE QPVESQPLLH QEASSTNPGD HPAPTYAPAQ QLELAEAKEA
SGPKQKTCQC CVVM
