ID   PALMD_RAT               Reviewed;         551 AA.
AC   Q4KM62;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Palmdelphin;
GN   Name=Palmd;
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 [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP   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   -!- SUBUNIT: Interacts with GLUL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16323283}. Cell
CC       projection, dendrite {ECO:0000269|PubMed:16323283}. Cell projection,
CC       dendritic spine {ECO:0000269|PubMed:16323283}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain and the spinal cord.
CC       Expressed in the anterior olfactory nucleus, the olfactory tubercle,
CC       the nucleus supraopticus, the nucleus of the lateral olfactory tract,
CC       the piriform cortex, the cortico-amygdaloid transition zone, the
CC       septofimbrial nucleus and the indusium griseum (at protein level).
CC       {ECO:0000269|PubMed:16323283}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR   EMBL; BC098755; AAH98755.1; -; mRNA.
DR   RefSeq; NP_001020859.1; NM_001025688.1.
DR   AlphaFoldDB; Q4KM62; -.
DR   SMR; Q4KM62; -.
DR   STRING; 10116.ENSRNOP00000022615; -.
DR   iPTMnet; Q4KM62; -.
DR   PhosphoSitePlus; Q4KM62; -.
DR   PaxDb; Q4KM62; -.
DR   PRIDE; Q4KM62; -.
DR   Ensembl; ENSRNOT00000095854; ENSRNOP00000090695; ENSRNOG00000058609.
DR   GeneID; 310811; -.
DR   KEGG; rno:310811; -.
DR   UCSC; RGD:1305624; rat.
DR   CTD; 54873; -.
DR   RGD; 1305624; Palmd.
DR   eggNOG; ENOG502QVMH; Eukaryota.
DR   GeneTree; ENSGT00940000157718; -.
DR   InParanoid; Q4KM62; -.
DR   OrthoDB; 275462at2759; -.
DR   PhylomeDB; Q4KM62; -.
DR   TreeFam; TF105402; -.
DR   PRO; PR:Q4KM62; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
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_0000262531"
FT   REGION          247..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..106
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        314..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..515
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         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         270
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         515
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
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"
SQ   SEQUENCE   551 AA;  62419 MW;  D87357FC92ABAA5F CRC64;
     MEEAELVKGR LQAITDKRKI QEEISQKRLK IEEEKLKHQH LKKKALREKW LLDGIGSGKE
     HDEMKKQNQQ DQHQTQVLEQ SILRLEKEIQ DLEKAELQIS ANEEVILKKL KSIERTTEDI
     IRSVKVEKEE IPEESIEDIY ANIPDLPSSY IPSRLRKERN EESDDEQNRK ALYAMEIKVE
     KDLKTGESVV LSSIPLPSDD FKSTGIKVYE DRQKSVYAVS SNQNTAYNGT DGLAPVEVED
     LLRQASERNS KSPTEYHEPV YANPFCRPMT PQRERVISPG PNSQERMVMM KANGLDHHES
     ESVHGMTDGL SERRSNGLAH TSPTRPTPQP RSKVQQVEEM VHTQQKRMPS PWEESSIRQN
     EYEVSPRTEL SPSRASPGKS GPQCSSPICQ EEADVRYNIV HSLPPDVDDT EPVTMIFMGY
     QQADENEEEK KLLTGYDGVI HAELVVIDDE AEDDEGQAEK PSYHPVAPCS QVYQPAKPTP
     LPRKRSEVSP HENTNHKSPH KNSISLKEQE ERLGSPARHS PLGVPGAGDG TEDPSLTALR
     IRMAKLGKKV I