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Paralemmin-3 (Developmental protein XlGV7) (Xlcaax-1)

 PALM3_XENLA             Reviewed;         591 AA.
P20398;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
07-JUN-2017, entry version 67.
RecName: Full=Paralemmin-3;
AltName: Full=Developmental protein XlGV7;
AltName: Full=Xlcaax-1;
Flags: Precursor;
Name=palm3; Synonyms=gv7;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2721962; DOI=10.1101/gad.3.4.572;
Miller M., Kloc M., Reddy B., Eastman E., Dreyer C., Etkin L.;
"xlgv7: a maternal gene product localized in nuclei of the central
nervous system in Xenopus laevis.";
Genes Dev. 3:572-583(1989).
[2]
ISOPRENYLATION AT CYS-588, PALMITOYLATION AT CYS-585 AND CYS-587, AND
SUBCELLULAR LOCATION.
PubMed=2022638;
Kloc M., Reddy B., Crawford S., Etkin L.D.;
"A novel 110-kDa maternal CAAX box-containing protein from Xenopus is
palmitoylated and isoprenylated when expressed in baculovirus.";
J. Biol. Chem. 266:8206-8212(1991).
[3]
SUBCELLULAR LOCATION, ATP-BINDING, ISOPRENYLATION AT CYS-588,
PALMITOYLATION AT CYS-585 AND CYS-587, AND MUTAGENESIS OF CYS-585;
CYS-587 AND CYS-588.
PubMed=8347620; DOI=10.1021/bi00083a022;
Kloc M., Li X.X., Etkin L.D.;
"Two upstream cysteines and the CAAX motif but not the polybasic
domain are required for membrane association of Xlcaax in Xenopus
oocytes.";
Biochemistry 32:8207-8212(1993).
-!- FUNCTION: Maternal ATP-binding protein that may have multiple
functions during development, one of which may be associated with
the development and maintenance of the central nervous system.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Lipid-
anchor. Note=Cytoplasmic (following oocyte maturation), then
nuclear (blastula/gastrula stage).
-!- TISSUE SPECIFICITY: In Xenopus oocyte, in the central nervous
system cells of tadpoles and adult frogs, and transiently in
epithelial cells of stomach and gut of tadpoles. Highly expressed
in kidney.
-!- DEVELOPMENTAL STAGE: Neurula stage and in adult brain.
-!- DOMAIN: The polybasic C-terminal domain is not required for
membrane localization.
-!- PTM: May be phosphorylated during oocyte maturation.
-!- PTM: Palmitoylated on Cys-585 and Cys-587 and prenylated on Cys-
588; which is required for membrane association.
{ECO:0000269|PubMed:2022638, ECO:0000269|PubMed:8347620}.
-!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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EMBL; X15627; CAA33637.1; -; mRNA.
PIR; A30098; A30098.
RefSeq; NP_001095233.1; NM_001101763.1.
UniGene; Xl.1204; -.
SMR; P20398; -.
PRIDE; P20398; -.
GeneID; 397899; -.
KEGG; xla:397899; -.
CTD; 342979; -.
HOVERGEN; HBG106678; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cytoplasm; Developmental protein;
Differentiation; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Prenylation;
Repeat.
CHAIN 1 588 Paralemmin-3.
/FTId=PRO_0000083880.
PROPEP 589 591 Removed in mature form.
/FTId=PRO_0000332175.
REPEAT 171 174
REPEAT 183 186
REPEAT 224 227
REPEAT 234 237
MOTIF 579 583 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 101 437 His-rich.
MOD_RES 588 588 Cysteine methyl ester. {ECO:0000305}.
LIPID 585 585 S-palmitoyl cysteine.
{ECO:0000269|PubMed:2022638,
ECO:0000269|PubMed:8347620}.
LIPID 587 587 S-palmitoyl cysteine.
{ECO:0000269|PubMed:2022638,
ECO:0000269|PubMed:8347620}.
LIPID 588 588 S-farnesyl cysteine.
{ECO:0000269|PubMed:2022638,
ECO:0000269|PubMed:8347620}.
MUTAGEN 585 585 C->S: Strongly reduces membrane
association.
{ECO:0000269|PubMed:8347620}.
MUTAGEN 587 587 C->S: Strongly reduces membrane
association.
{ECO:0000269|PubMed:8347620}.
MUTAGEN 588 588 C->S: Abolishes membrane association.
{ECO:0000269|PubMed:8347620}.
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


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