PALMD_MOUSE
ID PALMD_MOUSE Reviewed; 551 AA.
AC Q9JHU2; Q3TAG0; Q91X00; Q9D693;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Palmdelphin;
GN Name=Palmd;
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].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=11707320; DOI=10.1016/s0378-1119(01)00719-3;
RA Andreu N., Escarceller M., Feather S., Devriendt K., Wolf A.S.,
RA Estivill X., Sumoy L.;
RT "PALML, a novel paralemmin-related gene mapping on human chromosome 1p21.";
RL Gene 278:33-40(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG The European IMAGE consortium;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP FUNCTION, INTERACTION WITH GLUL, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16323283; DOI=10.1016/j.ejcb.2005.07.002;
RA Hu B., Petrasch-Parwez E., Laue M.M., Kilimann M.W.;
RT "Molecular characterization and immunohistochemical localization of
RT palmdelphin, a cytosolic isoform of the paralemmin protein family
RT implicated in membrane dynamics.";
RL Eur. J. Cell Biol. 84:853-866(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-375 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-349; SER-370;
RP SER-375; SER-384; SER-385; SER-515 AND SER-520, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, and
RC Spleen;
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 -!- SUBUNIT: Interacts with GLUL. {ECO:0000269|PubMed:16323283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, dendrite. Cell
CC projection, dendritic spine {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at highest levels in the
CC heart and lung. {ECO:0000269|PubMed:11478809}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16323283}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; AF263246; AAK48507.1; -; mRNA.
DR EMBL; AJ312215; CAC59696.1; -; mRNA.
DR EMBL; AL391037; CAC01530.1; -; mRNA.
DR EMBL; AK014531; BAB29414.1; -; mRNA.
DR EMBL; AK171869; BAE42708.1; -; mRNA.
DR EMBL; BC010193; AAH10193.1; -; mRNA.
DR CCDS; CCDS17793.1; -.
DR RefSeq; NP_075734.3; NM_023245.3.
DR AlphaFoldDB; Q9JHU2; -.
DR SMR; Q9JHU2; -.
DR BioGRID; 227669; 1.
DR STRING; 10090.ENSMUSP00000044693; -.
DR iPTMnet; Q9JHU2; -.
DR PhosphoSitePlus; Q9JHU2; -.
DR jPOST; Q9JHU2; -.
DR MaxQB; Q9JHU2; -.
DR PaxDb; Q9JHU2; -.
DR PRIDE; Q9JHU2; -.
DR ProteomicsDB; 294102; -.
DR DNASU; 114301; -.
DR GeneID; 114301; -.
DR KEGG; mmu:114301; -.
DR CTD; 54873; -.
DR MGI; MGI:2148896; Palmd.
DR eggNOG; ENOG502QVMH; Eukaryota.
DR InParanoid; Q9JHU2; -.
DR OrthoDB; 275462at2759; -.
DR PhylomeDB; Q9JHU2; -.
DR TreeFam; TF105402; -.
DR BioGRID-ORCS; 114301; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Palmd; mouse.
DR PRO; PR:Q9JHU2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JHU2; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Synapse; Ubl conjugation.
FT CHAIN 1..551
FT /note="Palmdelphin"
FT /id="PRO_0000262529"
FT REGION 247..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..106
FT /evidence="ECO:0000255"
FT COMPBIAS 294..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT CONFLICT 65
FT /note="R -> K (in Ref. 2; CAC59696 and 4; BAB29414/
FT BAE42708)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="P -> H (in Ref. 4; BAB29414)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="V -> I (in Ref. 4; BAE42708)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="N -> S (in Ref. 2; CAC59696 and 4; BAB29414/
FT BAE42708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 62700 MW; F4AE52C14BC2582C CRC64;
MEEAELVKGR LQAITDKRKI QEEISQKRLK IEEEKLKHQH LKKKALREKW LLDGIGSGKE
HEEMRKQNQQ DQHQTQVLEQ SILRLEKEIQ DLEKAELQIS ANEEAILKKL KSIEKTTEDI
IRSVKVEKEE NPEESIEDIY ANIPDLPSSY IPSRLRKERN EGPDDEQNRK ALYAMEIKVE
KDLKTGESVV LSSIPLPSDD FKSTGIKVYE DRQKSVYAVS SNQNTTYNGT DGLAPVEVED
LLRQASERNS KSPTEYHEPV YANPFCRPVT PQRERVISPG PNFQERIMMK TNGLGNHANE
SAHNMTDGLS ERRSNGPTHT SPTRPTPQPR SMVQQVEEMV HTQQKRMASP WEESSNRQNE
HEVSPRMELS PSRASPGKSG PQCSSPTCQE ETEDVRYNIV HSLPSDVDDT EPVTMIFMGY
QQADDNEEEK KLLTGYDGVI HAELVVIDDE AEDNEGQTER PSYHPVAPYN QVYQPPKPTP
LPRKRAEVRP YENTNHKSPH KNSISLKEQE ERLGSPARHS PLDVPVAGDG TEDPSLTALR
IRMAKLGKKV I
