PLLP_HUMAN
ID PLLP_HUMAN Reviewed; 182 AA.
AC Q9Y342; B2R9T6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Plasmolipin;
DE AltName: Full=Plasma membrane proteolipid;
GN Name=PLLP; Synonyms=PMLP, TM4SF11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Xie B., Durrie R., Sapirstein V.S.;
RT "Molecular cloning of human plasmolipin cDNA.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Hexamer arranged as a trimer of two plasmolipin subunits.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y342; Q13520: AQP6; NbExp=3; IntAct=EBI-3919291, EBI-13059134;
CC Q9Y342; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-3919291, EBI-747430;
CC Q9Y342; Q6UWJ8-2: CD164L2; NbExp=3; IntAct=EBI-3919291, EBI-13362802;
CC Q9Y342; O95500: CLDN14; NbExp=3; IntAct=EBI-3919291, EBI-11742599;
CC Q9Y342; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-3919291, EBI-12811991;
CC Q9Y342; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-3919291, EBI-11749983;
CC Q9Y342; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-3919291, EBI-17233035;
CC Q9Y342; A8MQ03: CYSRT1; NbExp=4; IntAct=EBI-3919291, EBI-3867333;
CC Q9Y342; Q15125: EBP; NbExp=3; IntAct=EBI-3919291, EBI-3915253;
CC Q9Y342; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-3919291, EBI-18535450;
CC Q9Y342; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3919291, EBI-781551;
CC Q9Y342; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-3919291, EBI-18636064;
CC Q9Y342; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3919291, EBI-12142257;
CC Q9Y342; O43559: FRS3; NbExp=3; IntAct=EBI-3919291, EBI-725515;
CC Q9Y342; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-3919291, EBI-17231387;
CC Q9Y342; Q8TED1: GPX8; NbExp=3; IntAct=EBI-3919291, EBI-11721746;
CC Q9Y342; P28799: GRN; NbExp=3; IntAct=EBI-3919291, EBI-747754;
CC Q9Y342; P49639: HOXA1; NbExp=3; IntAct=EBI-3919291, EBI-740785;
CC Q9Y342; P48051: KCNJ6; NbExp=3; IntAct=EBI-3919291, EBI-12017638;
CC Q9Y342; O76011: KRT34; NbExp=3; IntAct=EBI-3919291, EBI-1047093;
CC Q9Y342; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-3919291, EBI-1044640;
CC Q9Y342; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3919291, EBI-2820517;
CC Q9Y342; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3919291, EBI-11956541;
CC Q9Y342; Q9NXJ0: MS4A12; NbExp=6; IntAct=EBI-3919291, EBI-10227644;
CC Q9Y342; Q9H813: PACC1; NbExp=3; IntAct=EBI-3919291, EBI-4319734;
CC Q9Y342; O15173: PGRMC2; NbExp=3; IntAct=EBI-3919291, EBI-1050125;
CC Q9Y342; Q9H9V4: RNF122; NbExp=3; IntAct=EBI-3919291, EBI-2129998;
CC Q9Y342; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-3919291, EBI-3920694;
CC Q9Y342; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3919291, EBI-18159983;
CC Q9Y342; Q86WV6: STING1; NbExp=3; IntAct=EBI-3919291, EBI-2800345;
CC Q9Y342; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-3919291, EBI-18196631;
CC Q9Y342; Q495A1: TIGIT; NbExp=3; IntAct=EBI-3919291, EBI-4314807;
CC Q9Y342; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3919291, EBI-8638294;
CC Q9Y342; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-3919291, EBI-17684533;
CC Q9Y342; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-3919291, EBI-10276729;
CC Q9Y342; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-3919291, EBI-11724433;
CC Q9Y342; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-3919291, EBI-12345267;
CC Q9Y342; O43557: TNFSF14; NbExp=3; IntAct=EBI-3919291, EBI-524131;
CC Q9Y342; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-3919291, EBI-10262539;
CC Q9Y342; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-3919291, EBI-1055364;
CC Q9Y342; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-3919291, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
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DR EMBL; AF137386; AAD33060.1; -; mRNA.
DR EMBL; AK313910; BAG36633.1; -; mRNA.
DR EMBL; CH471092; EAW82915.1; -; Genomic_DNA.
DR EMBL; BC002760; AAH02760.1; -; mRNA.
DR CCDS; CCDS10777.1; -.
DR RefSeq; NP_057077.1; NM_015993.2.
DR AlphaFoldDB; Q9Y342; -.
DR BioGRID; 119279; 58.
DR IntAct; Q9Y342; 50.
DR MINT; Q9Y342; -.
DR STRING; 9606.ENSP00000219207; -.
DR iPTMnet; Q9Y342; -.
DR PhosphoSitePlus; Q9Y342; -.
DR BioMuta; PLLP; -.
DR DMDM; 12229882; -.
DR EPD; Q9Y342; -.
DR jPOST; Q9Y342; -.
DR MassIVE; Q9Y342; -.
DR MaxQB; Q9Y342; -.
DR PaxDb; Q9Y342; -.
DR PeptideAtlas; Q9Y342; -.
DR PRIDE; Q9Y342; -.
DR ProteomicsDB; 85972; -.
DR Antibodypedia; 44063; 105 antibodies from 20 providers.
DR DNASU; 51090; -.
DR Ensembl; ENST00000219207.10; ENSP00000219207.5; ENSG00000102934.10.
DR GeneID; 51090; -.
DR KEGG; hsa:51090; -.
DR MANE-Select; ENST00000219207.10; ENSP00000219207.5; NM_015993.3; NP_057077.1.
DR UCSC; uc002elg.3; human.
DR CTD; 51090; -.
DR DisGeNET; 51090; -.
DR GeneCards; PLLP; -.
DR HGNC; HGNC:18553; PLLP.
DR HPA; ENSG00000102934; Group enriched (brain, choroid plexus).
DR MIM; 600340; gene.
DR neXtProt; NX_Q9Y342; -.
DR OpenTargets; ENSG00000102934; -.
DR PharmGKB; PA38572; -.
DR VEuPathDB; HostDB:ENSG00000102934; -.
DR eggNOG; KOG4788; Eukaryota.
DR GeneTree; ENSGT00940000156011; -.
DR HOGENOM; CLU_103581_2_0_1; -.
DR InParanoid; Q9Y342; -.
DR OMA; WFNTVAM; -.
DR OrthoDB; 1455336at2759; -.
DR PhylomeDB; Q9Y342; -.
DR TreeFam; TF316174; -.
DR PathwayCommons; Q9Y342; -.
DR SignaLink; Q9Y342; -.
DR BioGRID-ORCS; 51090; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; PLLP; human.
DR GenomeRNAi; 51090; -.
DR Pharos; Q9Y342; Tbio.
DR PRO; PR:Q9Y342; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y342; protein.
DR Bgee; ENSG00000102934; Expressed in inferior vagus X ganglion and 183 other tissues.
DR ExpressionAtlas; Q9Y342; baseline and differential.
DR Genevisible; Q9Y342; HS.
DR GO; GO:0043218; C:compact myelin; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR InterPro; IPR013295; MAL.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 1.
DR PRINTS; PR01884; MALPROTEIN.
DR PROSITE; PS51225; MARVEL; 1.
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_0000156813"
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 MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 182 AA; 19987 MW; 6F09AA080E2F67E8 CRC64;
MAEFPSKVST RTSSPAQGAE ASVSALRPDL GFVRSRLGAL MLLQLVLGLL VWALIADTPY
HLYPAYGWVM FVAVFLWLVT IVLFNLYLFQ LHMKLYMVPW PLVLMIFNIS ATVLYITAFI
ACSAAVDLTS LRGTRPYNQR AAASFFACLV MIAYGVSAFF SYQAWRGVGS NAATSQMAGG
YA
