ID   PALMD_PIG               Reviewed;         551 AA.
AC   Q2MJV9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Palmdelphin;
GN   Name=PALMD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Neumann N.G., Kilimann M.W.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Interacts with GLUL (By similarity). Cell projection,
CC       dendrite. Cell projection, dendritic spine (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC       dendrite. Cell projection, dendritic spine {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR   EMBL; DQ322458; ABC49999.1; -; mRNA.
DR   RefSeq; NP_001033734.1; NM_001038645.2.
DR   AlphaFoldDB; Q2MJV9; -.
DR   SMR; Q2MJV9; -.
DR   STRING; 9823.ENSSSCP00000007329; -.
DR   PaxDb; Q2MJV9; -.
DR   PeptideAtlas; Q2MJV9; -.
DR   PRIDE; Q2MJV9; -.
DR   GeneID; 654413; -.
DR   KEGG; ssc:654413; -.
DR   CTD; 54873; -.
DR   eggNOG; ENOG502QVMH; Eukaryota.
DR   InParanoid; Q2MJV9; -.
DR   OrthoDB; 275462at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript 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_0000262530"
FT   REGION          247..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2..106
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        300..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..507
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         271
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHU2"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         385
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        179
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   CROSSLNK        179
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;  62308 MW;  F6013DCE8FF644EC CRC64;
     MEEAELVKER LQAITDKRKI QEEISQKRLK IEEEKLRHQH LKKKALREKW LLDGIGSRKE
     QEEMKKQNQQ DQHQIQVLEQ SILRLEKEIQ DLEKAELQIS TNEEAILKKL KSVERTTEDI
     IRSVKVEKEE TSGASIEDIY ANIPDLPKSY VPSRLRKERN EGIEDDEQNR KALYAMEIKV
     EKDLKTGEST VLSSIPLPSD DFKGTGIKVY DDGQKSVYAV SSNHSAAYNG TDGLAPVEVE
     DLLRQASERN SKSPTEYHDP VYANPFCRPT TPQREKATPG PNFQERIKMK ARGLGKDMNG
     SIHTMNNGLS EERGSSVNHI SPIRPIPHPR SMTQQAEERP HSPQKRQMTP WEESDVTQDK
     CAPSAKSQLS PGEAPVGKSE RQGSSPTCQE DEEDVRYNIV HSLPSDVEDT EPVTMIFMGY
     QRADDSEEEK KLLTGYDGII RAELVVIDDE EEEGEGEAEK PSYHPIAPHS QVFQPAKPTP
     LPRKRAEVNP HENTNHKSPH KNSISLKEQE ESLGSPIHQS PLDIQIAGDG TEDPSLTALR
     MRMAKLGKKV I