ID   PALMD_BOVIN             Reviewed;         550 AA.
AC   Q3MHH7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Palmdelphin;
GN   Name=PALMD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Interacts with GLUL. {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; BC105234; AAI05235.1; -; mRNA.
DR   RefSeq; NP_001030251.1; NM_001035079.2.
DR   AlphaFoldDB; Q3MHH7; -.
DR   SMR; Q3MHH7; -.
DR   STRING; 9913.ENSBTAP00000023485; -.
DR   PaxDb; Q3MHH7; -.
DR   PRIDE; Q3MHH7; -.
DR   GeneID; 509823; -.
DR   KEGG; bta:509823; -.
DR   CTD; 54873; -.
DR   eggNOG; ENOG502QVMH; Eukaryota.
DR   InParanoid; Q3MHH7; -.
DR   OrthoDB; 275462at2759; -.
DR   Proteomes; UP000009136; 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..550
FT                   /note="Palmdelphin"
FT                   /id="PRO_0000262527"
FT   REGION          248..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2..106
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        483..506
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         497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP74"
FT   MOD_RES         519
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   550 AA;  62380 MW;  8284B3314BF12F3F CRC64;
     MEEAELVKER LQAITDKRKI QEEISQKRLK IEEEKLKHQH LKKKALREKW LLDGISSGKE
     QEEMKKQNQQ DQHQIQVLEQ SILRLEKEIQ DLEKAELQIS TNEEAILKKL KSVERTTEDI
     IRSVKVEKEE TSGESVEDIY ANIPDLPKSY IPSRLRKERN EGIEDDEQNR KALYAMEIKV
     EKDLKTGEST VLSSIPLPSD DFKGTGIKVY DDGQKSVYAV SSNHSAAYNG TDGLAPVEVE
     ELLRQASERN SKSPTEYHEP VYANPFCRPT TPQREKVTPG PNFQERVKIK ANGLGNDVNG
     SIHNIDNGLA EERGNNVNHI SPARPIPHPR SMIQQAEEMP HIQQERLMTP WEEPNVMQDK
     YTPSPKSGLS PSRALVEKSE RQSSSPPCQE DEKDIRYNIV HSLPSDLDEK EPVTMIFMGY
     QQAEDNEEEK KLLTGYDGII HAELVVIDDE EEGEGEAEKP AYHPIAPHSQ VFQPAKPTPL
     PRKRAEVNPH ENTNHKSPHK NSISLKEQEE SLGSPIHHSP LDVQIAGDGT EDPSLTALRM
     RMAKLGKKVI