STML1_HUMAN
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 03-AUG-2022, entry version 157.
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};
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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; 9.
DR IntAct; Q9UBI4; 5.
DR STRING; 9606.ENSP00000442478; -.
DR iPTMnet; Q9UBI4; -.
DR PhosphoSitePlus; Q9UBI4; -.
DR BioMuta; STOML1; -.
DR DMDM; 60415942; -.
DR EPD; Q9UBI4; -.
DR jPOST; Q9UBI4; -.
DR MassIVE; Q9UBI4; -.
DR MaxQB; Q9UBI4; -.
DR PaxDb; Q9UBI4; -.
DR PeptideAtlas; Q9UBI4; -.
DR PRIDE; Q9UBI4; -.
DR ProteomicsDB; 17957; -.
DR ProteomicsDB; 42124; -.
DR ProteomicsDB; 5218; -.
DR ProteomicsDB; 83973; -. [Q9UBI4-1]
DR ProteomicsDB; 83974; -. [Q9UBI4-2]
DR Antibodypedia; 26821; 135 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 CTD; 9399; -.
DR DisGeNET; 9399; -.
DR GeneCards; STOML1; -.
DR HGNC; HGNC:14560; STOML1.
DR HPA; ENSG00000067221; Low tissue specificity.
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; 1062075at2759; -.
DR PhylomeDB; Q9UBI4; -.
DR TreeFam; TF105750; -.
DR PathwayCommons; Q9UBI4; -.
DR SignaLink; Q9UBI4; -.
DR BioGRID-ORCS; 9399; 7 hits in 1080 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 197 other tissues.
DR ExpressionAtlas; Q9UBI4; baseline and differential.
DR Genevisible; Q9UBI4; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.30.1050.10; -; 1.
DR Gene3D; 3.30.479.30; -; 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_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
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
