ID STML1_HUMAN Reviewed; 398 AA. AC Q9UBI4; B3KQN0; B4DUU5; B4DXM9; E7ESC0; H3BRP3; O95675; Q4PNR4; Q6FGL8; AC Q8WYI7; Q9UMB9; Q9UMC0; Q9Y6H9; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 164. DE RecName: Full=Stomatin-like protein 1; DE Short=SLP-1; DE AltName: Full=EPB72-like protein 1; DE AltName: Full=Protein unc-24 homolog; DE AltName: Full=Stomatin-related protein; DE Short=STORP; GN Name=STOML1; Synonyms=SLP1, UNC24; ORFNames=MSTP019; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain cortex; RX PubMed=9931417; DOI=10.1016/s0378-1119(98)00532-0; RA Seidel G., Prohaska R.; RT "Molecular cloning of hSLP-1, a novel human brain-specific member of the RT band 7/MEC-2 family similar to Caenorhabditis elegans UNC-24."; RL Gene 225:23-29(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal liver; RX PubMed=10997330; DOI=10.1034/j.1600-0609.2000.90054.x; RA Gilles F., Glenn M., Goy A., Remache Y., Zelenetz A.D.; RT "A novel gene STORP (STOmatin-Related Protein) is localized 2 kb upstream RT of the promyelocytic gene on chromosome 15q22."; RL Eur. J. Haematol. 64:104-113(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Aorta; RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J.-W., Wei Y.J., Sun Y.H., RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Wen S., Lin L., Yang S.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). RC TISSUE=Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thyroid; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Lung; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-398 (ISOFORM 3). RA Barnes T.M., Benard C., Hekimi S.; RT "UNC-24/hunc-24 implicates stomatin and stomatin-like proteins in the RT function of the lipid bilayer."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-398 (ISOFORM 4). RG The European IMAGE consortium; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [13] RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH STOM, AND MUTAGENESIS OF RP TYR-7 AND LEU-10. RX PubMed=19696025; DOI=10.1074/jbc.m109.014993; RA Mairhofer M., Steiner M., Salzer U., Prohaska R.; RT "Stomatin-like protein-1 interacts with stomatin and is targeted to late RT endosomes."; RL J. Biol. Chem. 284:29218-29229(2009). RN [14] RP INTERACTION WITH FBXW7 AND CDK2, AND FUNCTION. RX PubMed=23082202; DOI=10.1371/journal.pone.0047736; RA Zhang W., MacDonald E.M., Koepp D.M.; RT "The stomatin-like protein SLP-1 and Cdk2 interact with the F-Box protein RT Fbw7-gamma."; RL PLoS ONE 7:E47736-E47736(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; 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: May play a role in cholesterol transfer to late endosomes CC (PubMed:19696025). May play a role in modulating membrane acid-sensing CC ion channels. Can specifically inhibit proton-gated current of ASIC1 CC isoform 1. Can increase inactivation speed of ASIC3. May be involved in CC regulation of proton sensing in dorsal root ganglions (By similarity). CC May play a role in protecting FBXW7 isoform 3 from degradation CC (PubMed:23082202). {ECO:0000250|UniProtKB:Q8CI66, CC ECO:0000269|PubMed:19696025, ECO:0000305|PubMed:23082202}. CC -!- SUBUNIT: Interacts with STOM; may redistribute STOM from the plasma CC membrane to late endosomes (PubMed:19696025). Interacts with FBXW7 CC isoform 3 and CDK2 (PubMed:23082202). {ECO:0000269|PubMed:19696025, CC ECO:0000269|PubMed:23082202}. CC -!- INTERACTION: CC Q9UBI4; P24941: CDK2; NbExp=2; IntAct=EBI-2681162, EBI-375096; CC Q9UBI4; Q969H0-4: FBXW7; NbExp=3; IntAct=EBI-2681162, EBI-6502391; CC Q9UBI4; P27105: STOM; NbExp=4; IntAct=EBI-2681162, EBI-1211440; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III CC membrane protein {ECO:0000305}. Late endosome membrane CC {ECO:0000269|PubMed:19696025}. Membrane raft CC {ECO:0000269|PubMed:19696025}. Cell membrane CC {ECO:0000250|UniProtKB:Q8CI66}; Single-pass type III membrane protein. CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8CI66}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9UBI4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBI4-2; Sequence=VSP_012654; CC Name=3; CC IsoId=Q9UBI4-3; Sequence=VSP_054649; CC Name=4; CC IsoId=Q9UBI4-4; Sequence=VSP_012654, VSP_054649; CC Name=5; CC IsoId=Q9UBI4-5; Sequence=VSP_054648, VSP_054649; CC Name=6; CC IsoId=Q9UBI4-6; Sequence=VSP_054649, VSP_054650; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Expression is CC highest in brain. {ECO:0000269|PubMed:10997330, CC ECO:0000269|PubMed:9931417}. CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD42031.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA76271.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y16522; CAA76271.1; ALT_FRAME; mRNA. DR EMBL; AF156564; AAF23080.1; -; Genomic_DNA. DR EMBL; AF156558; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156560; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156559; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156563; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156562; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156561; AAF23080.1; JOINED; Genomic_DNA. DR EMBL; AF156557; AAF06960.1; -; mRNA. DR EMBL; AF111800; AAL39002.1; -; mRNA. DR EMBL; DQ064605; AAY68393.1; -; mRNA. DR EMBL; CR542089; CAG46886.1; -; mRNA. DR EMBL; AK300799; BAG62457.1; -; mRNA. DR EMBL; AK302051; BAG63441.1; -; mRNA. DR EMBL; AK075244; BAG52092.1; -; mRNA. DR EMBL; AC108137; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77940.1; -; Genomic_DNA. DR EMBL; CH471082; EAW77944.1; -; Genomic_DNA. DR EMBL; BC034379; AAH34379.1; -; mRNA. DR EMBL; BC065249; AAH65249.1; -; mRNA. DR EMBL; AF074953; AAD42031.1; ALT_FRAME; mRNA. DR EMBL; AL109664; CAB52015.1; -; mRNA. DR EMBL; AL109665; CAB52016.1; -; mRNA. DR CCDS; CCDS10254.1; -. [Q9UBI4-1] DR CCDS; CCDS58382.1; -. [Q9UBI4-5] DR CCDS; CCDS58383.1; -. [Q9UBI4-4] DR CCDS; CCDS58384.1; -. [Q9UBI4-2] DR CCDS; CCDS58385.1; -. [Q9UBI4-6] DR RefSeq; NP_001243601.1; NM_001256672.1. [Q9UBI4-3] DR RefSeq; NP_001243602.1; NM_001256673.1. [Q9UBI4-2] DR RefSeq; NP_001243603.1; NM_001256674.1. [Q9UBI4-4] DR RefSeq; NP_001243604.1; NM_001256675.1. [Q9UBI4-6] DR RefSeq; NP_001243605.1; NM_001256676.1. DR RefSeq; NP_001243606.1; NM_001256677.1. [Q9UBI4-5] DR RefSeq; NP_004800.2; NM_004809.4. [Q9UBI4-1] DR RefSeq; XP_006720836.1; XM_006720773.3. DR AlphaFoldDB; Q9UBI4; -. DR SMR; Q9UBI4; -. DR BioGRID; 114796; 10. DR IntAct; Q9UBI4; 6. DR STRING; 9606.ENSP00000442478; -. DR iPTMnet; Q9UBI4; -. DR PhosphoSitePlus; Q9UBI4; -. DR SwissPalm; Q9UBI4; -. DR BioMuta; STOML1; -. DR DMDM; 60415942; -. DR EPD; Q9UBI4; -. DR jPOST; Q9UBI4; -. DR MassIVE; Q9UBI4; -. DR MaxQB; Q9UBI4; -. DR PaxDb; 9606-ENSP00000442478; -. DR PeptideAtlas; Q9UBI4; -. DR ProteomicsDB; 17957; -. DR ProteomicsDB; 42124; -. DR ProteomicsDB; 5218; -. DR ProteomicsDB; 83973; -. [Q9UBI4-1] DR ProteomicsDB; 83974; -. [Q9UBI4-2] DR Antibodypedia; 26821; 143 antibodies from 21 providers. DR DNASU; 9399; -. DR Ensembl; ENST00000316900.9; ENSP00000319323.6; ENSG00000067221.14. [Q9UBI4-5] DR Ensembl; ENST00000316911.10; ENSP00000319384.6; ENSG00000067221.14. [Q9UBI4-2] DR Ensembl; ENST00000359750.8; ENSP00000352788.4; ENSG00000067221.14. [Q9UBI4-6] DR Ensembl; ENST00000541638.6; ENSP00000442478.2; ENSG00000067221.14. [Q9UBI4-1] DR Ensembl; ENST00000564777.5; ENSP00000456343.1; ENSG00000067221.14. [Q9UBI4-4] DR GeneID; 9399; -. DR KEGG; hsa:9399; -. DR MANE-Select; ENST00000541638.6; ENSP00000442478.2; NM_004809.5; NP_004800.2. DR UCSC; uc002awe.5; human. [Q9UBI4-1] DR AGR; HGNC:14560; -. DR CTD; 9399; -. DR DisGeNET; 9399; -. DR GeneCards; STOML1; -. DR HGNC; HGNC:14560; STOML1. DR HPA; ENSG00000067221; Tissue enhanced (brain). DR MIM; 608326; gene. DR neXtProt; NX_Q9UBI4; -. DR OpenTargets; ENSG00000067221; -. DR PharmGKB; PA37898; -. DR VEuPathDB; HostDB:ENSG00000067221; -. DR eggNOG; KOG2621; Eukaryota. DR eggNOG; KOG4170; Eukaryota. DR GeneTree; ENSGT01030000234614; -. DR HOGENOM; CLU_049498_0_0_1; -. DR InParanoid; Q9UBI4; -. DR OMA; AMHFLSH; -. DR OrthoDB; 2878294at2759; -. DR PhylomeDB; Q9UBI4; -. DR TreeFam; TF105750; -. DR PathwayCommons; Q9UBI4; -. DR SignaLink; Q9UBI4; -. DR BioGRID-ORCS; 9399; 7 hits in 1161 CRISPR screens. DR ChiTaRS; STOML1; human. DR GeneWiki; STOML1; -. DR GenomeRNAi; 9399; -. DR Pharos; Q9UBI4; Tbio. DR PRO; PR:Q9UBI4; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9UBI4; Protein. DR Bgee; ENSG00000067221; Expressed in pancreatic ductal cell and 199 other cell types or tissues. DR ExpressionAtlas; Q9UBI4; baseline and differential. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR CDD; cd13436; SPFH_SLP-1; 1. DR Gene3D; 3.30.479.30; Band 7 domain; 1. DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1. DR InterPro; IPR043202; Band-7_stomatin-like. DR InterPro; IPR001107; Band_7. DR InterPro; IPR036013; Band_7/SPFH_dom_sf. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf. DR InterPro; IPR001972; Stomatin_HflK_fam. DR PANTHER; PTHR10264; BAND 7 PROTEIN-RELATED; 1. DR PANTHER; PTHR10264:SF130; STOMATIN-LIKE PROTEIN 1; 1. DR Pfam; PF01145; Band_7; 1. DR Pfam; PF02036; SCP2; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; Band 7/SPFH domain; 1. DR SUPFAM; SSF55718; SCP-like; 1. DR Genevisible; Q9UBI4; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasmic vesicle; Endosome; KW Lipid transport; Membrane; Phosphoprotein; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..398 FT /note="Stomatin-like protein 1" FT /id="PRO_0000094029" FT TRANSMEM 58..78 FT /note="Helical; Signal-anchor for type III membrane FT protein" FT /evidence="ECO:0000255" FT TOPO_DOM 79..398 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 287..398 FT /note="SCP2" FT MOTIF 6..10 FT /note="Tyrosine-type lysosomal sorting signal" FT /evidence="ECO:0000255, ECO:0000269|PubMed:19696025" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..44 FT /note="MLGRSGYRALPLGDFDRFQQSSFGFLGSQKGCLSPERGGVGTGA -> MP FT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054648" FT VAR_SEQ 80..129 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.12, FT ECO:0000303|Ref.3" FT /id="VSP_012654" FT VAR_SEQ 264 FT /note="Missing (in isoform 3, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.11, FT ECO:0000303|Ref.12, ECO:0000303|Ref.4" FT /id="VSP_054649" FT VAR_SEQ 265..334 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_054650" FT MUTAGEN 7 FT /note="Y->A: Plasma membrane localization." FT /evidence="ECO:0000269|PubMed:19696025" FT MUTAGEN 10 FT /note="L->S: Plasma membrane localization." FT /evidence="ECO:0000269|PubMed:19696025" FT CONFLICT 50 FT /note="W -> G (in Ref. 5; CAG46886)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="V -> L (in Ref. 3; AAL39002)" FT /evidence="ECO:0000305" FT CONFLICT 291 FT /note="A -> T (in Ref. 5; CAG46886)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="P -> R (in Ref. 1; CAA76271)" FT /evidence="ECO:0000305" SQ SEQUENCE 398 AA; 42968 MW; A9850C26394E1C3D CRC64; MLGRSGYRAL PLGDFDRFQQ SSFGFLGSQK GCLSPERGGV GTGADVPQSW PSCLCHGLIS FLGFLLLLVT FPISGWFALK IVPTYERMIV FRLGRIRTPQ GPGMVLLLPF IDSFQRVDLR TRAFNVPPCK LASKDGAVLS VGADVQFRIW DPVLSVMTVK DLNTATRMTA QNAMTKALLK RPLREIQMEK LKISDQLLLE INDVTRAWGL EVDRVELAVE AVLQPPQDSP AGPNLDSTLQ QLALHFLGGS MNSMAGGAPS PGPADTVEMV SEVEPPAPQV GARSSPKQPL AEGLLTALQP FLSEALVSQV GACYQFNVVL PSGTQSAYFL DLTTGRGRVG HGVPDGIPDV VVEMAEADLR ALLCRELRPL GAYMSGRLKV KGDLAMAMKL EAVLRALK //