ID   PALM3_XENLA             Reviewed;         591 AA.
AC   P20398;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Paralemmin-3;
DE   AltName: Full=Developmental protein XlGV7;
DE   AltName: Full=Xlcaax-1;
DE   Flags: Precursor;
GN   Name=palm3; Synonyms=gv7;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2721962; DOI=10.1101/gad.3.4.572;
RA   Miller M., Kloc M., Reddy B., Eastman E., Dreyer C., Etkin L.;
RT   "xlgv7: a maternal gene product localized in nuclei of the central nervous
RT   system in Xenopus laevis.";
RL   Genes Dev. 3:572-583(1989).
RN   [2]
RP   ISOPRENYLATION AT CYS-588, PALMITOYLATION AT CYS-585 AND CYS-587, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=2022638; DOI=10.1016/s0021-9258(18)92962-5;
RA   Kloc M., Reddy B., Crawford S., Etkin L.D.;
RT   "A novel 110-kDa maternal CAAX box-containing protein from Xenopus is
RT   palmitoylated and isoprenylated when expressed in baculovirus.";
RL   J. Biol. Chem. 266:8206-8212(1991).
RN   [3]
RP   SUBCELLULAR LOCATION, ATP-BINDING, ISOPRENYLATION AT CYS-588,
RP   PALMITOYLATION AT CYS-585 AND CYS-587, AND MUTAGENESIS OF CYS-585; CYS-587
RP   AND CYS-588.
RX   PubMed=8347620; DOI=10.1021/bi00083a022;
RA   Kloc M., Li X.X., Etkin L.D.;
RT   "Two upstream cysteines and the CAAX motif but not the polybasic domain are
RT   required for membrane association of Xlcaax in Xenopus oocytes.";
RL   Biochemistry 32:8207-8212(1993).
CC   -!- FUNCTION: Maternal ATP-binding protein that may have multiple functions
CC       during development, one of which may be associated with the development
CC       and maintenance of the central nervous system.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Lipid-anchor.
CC       Note=Cytoplasmic (following oocyte maturation), then nuclear
CC       (blastula/gastrula stage).
CC   -!- TISSUE SPECIFICITY: In Xenopus oocyte, in the central nervous system
CC       cells of tadpoles and adult frogs, and transiently in epithelial cells
CC       of stomach and gut of tadpoles. Highly expressed in kidney.
CC   -!- DEVELOPMENTAL STAGE: Neurula stage and in adult brain.
CC   -!- DOMAIN: The polybasic C-terminal domain is not required for membrane
CC       localization.
CC   -!- PTM: May be phosphorylated during oocyte maturation.
CC   -!- PTM: Palmitoylated on Cys-585 and Cys-587 and prenylated on Cys-588;
CC       which is required for membrane association.
CC       {ECO:0000269|PubMed:2022638, ECO:0000269|PubMed:8347620}.
CC   -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR   EMBL; X15627; CAA33637.1; -; mRNA.
DR   PIR; A30098; A30098.
DR   RefSeq; NP_001095233.1; NM_001101763.1.
DR   AlphaFoldDB; P20398; -.
DR   GeneID; 397899; -.
DR   KEGG; xla:397899; -.
DR   CTD; 397899; -.
DR   Xenbase; XB-GENE-22041745; palm3.L.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 397899; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Nucleus; Palmitate; Phosphoprotein; Prenylation; Reference proteome;
KW   Repeat.
FT   CHAIN           1..588
FT                   /note="Paralemmin-3"
FT                   /id="PRO_0000083880"
FT   PROPEP          589..591
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000332175"
FT   REPEAT          171..174
FT   REPEAT          183..186
FT   REPEAT          224..227
FT   REPEAT          234..237
FT   REGION          282..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           579..583
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        282..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         588
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           585
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:2022638,
FT                   ECO:0000269|PubMed:8347620"
FT   LIPID           587
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:2022638,
FT                   ECO:0000269|PubMed:8347620"
FT   LIPID           588
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:2022638,
FT                   ECO:0000269|PubMed:8347620"
FT   MUTAGEN         585
FT                   /note="C->S: Strongly reduces membrane association."
FT                   /evidence="ECO:0000269|PubMed:8347620"
FT   MUTAGEN         587
FT                   /note="C->S: Strongly reduces membrane association."
FT                   /evidence="ECO:0000269|PubMed:8347620"
FT   MUTAGEN         588
FT                   /note="C->S: Abolishes membrane association."
FT                   /evidence="ECO:0000269|PubMed:8347620"
SQ   SEQUENCE   591 AA;  66174 MW;  9F3364CE52B3B540 CRC64;
     MSLQQLKRKS LRDGWLMDGV VPSPGAEIDS PLFQTESKIQ QLEKELESLQ MQQLRLENPA
     AVQPEAKAIQ TPFLNGEKIQ QGGGQAGDAK EVTAGQANNT HGIIHEEQPT KEDQDMGTVL
     PIPAPRGKTV PKEDENQANP ELKVDMEHQK VELVDLIQEC PVENQTVEHV EKNKPHLDQE
     HTEKNQDGQH GILEFLTQDQ QLGNPNLQHL DRYLITEVTV KHFEKNQAHP GQEKNQDEQH
     GILKYLTQDQ QNENPNLGHL DQYLITEITL QSNPLENISV HDQTQSTSDQ NMETKLPTDI
     PQQKESQSEG KIQTKDQGPE FELLYKDHSH EKGTTDQTQH QELLPSSIEP KEENPKAQDE
     KLDHHNESVS TVHEQKEVHD MDPRQLSTHQ KSLSISEDQN QGSVSLSDPQ NQDQSLALPE
     KGLEETPQLN LSHEVQCEEP SLMEQISISL LQSMEQNQEG ADQTPKSVAL EELSELLSSD
     MIKQSVLLSK NLEESPSTAS TEETQETMCQ AVIIPDLKKE NSDPEVVQES SSHEPMSSTI
     AQSSSAEGNS SPESRPLLQK SQGTDSQQGG NTATQQEERR KKKTCQCCVV M