ID   PLLP_RAT                Reviewed;         182 AA.
AC   P47987;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Plasmolipin;
DE   AltName: Full=Plasma membrane proteolipid;
GN   Name=Pllp; Synonyms=Pmlp, Tm4sf11;
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 [MRNA], AND CHARACTERIZATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=7929173; DOI=10.1016/s0021-9258(17)31477-1;
RA   Fischer I., Sapirstein V.S.;
RT   "Molecular cloning of plasmolipin. Characterization of a novel proteolipid
RT   restricted to brain and kidney.";
RL   J. Biol. Chem. 269:24912-24919(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=Wistar; TISSUE=Sciatic nerve;
RX   PubMed=8714710; DOI=10.1111/j.1460-9568.1996.tb01223.x;
RA   Gillen C., Gleichmann M., Greiner-Petter R., Zoidl G., Kupfer S., Bosse F.,
RA   Auer J., Mueller H.W.;
RT   "Full-lenth cloning, expression and cellular localization of rat
RT   plasmolipin mRNA, a proteolipid of PNS and CNS.";
RL   Eur. J. Neurosci. 8:405-414(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   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   -!- FUNCTION: Appears to be involved in myelination. Could also participate
CC       in ion transport events as addition of plasmolipin to lipid bilayers
CC       induces the formation of ion channels, which are voltage-dependent and
CC       K(+)-selective.
CC   -!- SUBUNIT: Hexamer arranged as a trimer of two plasmolipin subunits.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8714710}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:8714710}.
CC   -!- TISSUE SPECIFICITY: Expression restricted to the sciatic nerve, brain
CC       and kidney. In the sciatic nerve, found in Schwann cells; in the brain,
CC       in developing oligodendrocytes, especially of the corpus callosum, of
CC       cortical white matter, in the optic nerve and in the stratum radiatum
CC       and stratum oriens of the hippocampus. In kidney, segregated to the
CC       apical surface of renal tubular epithelia.
CC   -!- DEVELOPMENTAL STAGE: In the sciatic nerve, first detected at postnatal
CC       day P4, increases to a maximum at day P14 and then declines to moderate
CC       levels in adulthood. In the brain, onset of expression is at day P1,
CC       levels increase to reach a maximum at P20 and decline slightly to
CC       adulthood.
CC   -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U13617; AAA62133.1; ALT_INIT; mRNA.
DR   EMBL; Z49858; CAA90017.1; -; mRNA.
DR   EMBL; BC078823; AAH78823.1; -; mRNA.
DR   PIR; A55046; A55046.
DR   RefSeq; NP_071978.1; NM_022533.1.
DR   AlphaFoldDB; P47987; -.
DR   SMR; P47987; -.
DR   BioGRID; 249048; 1.
DR   STRING; 10116.ENSRNOP00000022277; -.
DR   TCDB; 1.A.64.1.1; the plasmolipin (plasmolipin) family.
DR   iPTMnet; P47987; -.
DR   PhosphoSitePlus; P47987; -.
DR   PaxDb; 10116-ENSRNOP00000022277; -.
DR   Ensembl; ENSRNOT00000022277.4; ENSRNOP00000022277.2; ENSRNOG00000016558.4.
DR   Ensembl; ENSRNOT00055038064; ENSRNOP00055031057; ENSRNOG00055022150.
DR   Ensembl; ENSRNOT00060027593; ENSRNOP00060022171; ENSRNOG00060016116.
DR   Ensembl; ENSRNOT00065005282; ENSRNOP00065003814; ENSRNOG00065003642.
DR   GeneID; 64364; -.
DR   KEGG; rno:64364; -.
DR   UCSC; RGD:621478; rat.
DR   AGR; RGD:621478; -.
DR   CTD; 51090; -.
DR   RGD; 621478; Pllp.
DR   eggNOG; KOG4788; Eukaryota.
DR   GeneTree; ENSGT00940000156011; -.
DR   HOGENOM; CLU_103581_2_0_1; -.
DR   InParanoid; P47987; -.
DR   OMA; PWPLVFM; -.
DR   OrthoDB; 5318078at2759; -.
DR   PhylomeDB; P47987; -.
DR   TreeFam; TF316174; -.
DR   PRO; PR:P47987; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000016558; Expressed in stomach and 17 other cell types or tissues.
DR   GO; GO:0043218; C:compact myelin; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IDA:RGD.
DR   GO; GO:0042552; P:myelination; IEP:RGD.
DR   InterPro; IPR013295; MAL.
DR   InterPro; IPR008253; Marvel.
DR   PANTHER; PTHR22776; MARVEL-CONTAINING POTENTIAL LIPID RAFT-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR22776:SF9; PLASMOLIPIN; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   PRINTS; PR01884; MALPROTEIN.
DR   PROSITE; PS51225; MARVEL; 1.
DR   Genevisible; P47987; RN.
PE   1: Evidence at protein level;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..182
FT                   /note="Plasmolipin"
FT                   /id="PRO_0000156815"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..68
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..166
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   182 AA;  19834 MW;  18F5844F9AA79F6E CRC64;
     MAEFPSKVST RTSSPAQGVG ASVSAMRPDL GFVRSALGVL ALLQLVLGLL VWALIADTPY
     HLYPAYGWVM FVAVFLWLVT IVFFIIYLFQ LHMKLYMVPW PLVLLVFFVA ATVLYITAFV
     ACAAAVDLTS LRGSRPYNQR SAASFFACLV MIAYGLSAFF SFQAWRGVGS NAATSQMAGG
     YS
//