TM165_HUMAN
ID TM165_HUMAN Reviewed; 324 AA.
AC Q9HC07; A8K3P8; B4DHW1; Q9BTN9; Q9NZ34;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transmembrane protein 165;
DE AltName: Full=Transmembrane protein PT27;
DE AltName: Full=Transmembrane protein TPARL;
DE Flags: Precursor;
GN Name=TMEM165; Synonyms=TPARL;
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).
RA Yue P., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Mus musculus transmembrane
RT protein.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, and Uterus;
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-124; LEU-127 AND 209-LEU-LEU-210,
RP CHARACTERIZATION OF VARIANTS CDG2K HIS-126; CYS-126 AND ARG-304, AND
RP TOPOLOGY.
RX PubMed=23575229; DOI=10.1093/hmg/ddt146;
RA Rosnoblet C., Legrand D., Demaegd D., Hacine-Gherbi H., de Bettignies G.,
RA Bammens R., Borrego C., Duvet S., Morsomme P., Matthijs G., Foulquier F.;
RT "Impact of disease-causing mutations on TMEM165 subcellular localization, a
RT recently identified protein involved in CDG-II.";
RL Hum. Mol. Genet. 22:2914-2928(2013).
RN [9]
RP INVOLVEMENT IN CDG2K.
RX PubMed=23430531; DOI=10.1007/8904_2012_172;
RA Zeevaert R., de Zegher F., Sturiale L., Garozzo D., Smet M., Moens M.,
RA Matthijs G., Jaeken J.;
RT "Bone dysplasia as a key feature in three patients with a novel congenital
RT disorder of glycosylation (CDG) type II due to a deep intronic splice
RT mutation in TMEM165.";
RL JIMD Rep. 8:145-152(2013).
RN [10]
RP FUNCTION IN CALCIUM AND PH HOMEOSTASIS.
RX PubMed=23569283; DOI=10.1073/pnas.1219871110;
RA Demaegd D., Foulquier F., Colinet A.S., Gremillon L., Legrand D.,
RA Mariot P., Peiter E., Van Schaftingen E., Matthijs G., Morsomme P.;
RT "Newly characterized Golgi-localized family of proteins is involved in
RT calcium and pH homeostasis in yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6859-6864(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP VARIANTS CDG2K HIS-126; CYS-126 AND ARG-304, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22683087; DOI=10.1016/j.ajhg.2012.05.002;
RA Foulquier F., Amyere M., Jaeken J., Zeevaert R., Schollen E., Race V.,
RA Bammens R., Morelle W., Rosnoblet C., Legrand D., Demaegd D., Buist N.,
RA Cheillan D., Guffon N., Morsomme P., Annaert W., Freeze H.H.,
RA Van Schaftingen E., Vikkula M., Matthijs G.;
RT "TMEM165 deficiency causes a congenital disorder of glycosylation.";
RL Am. J. Hum. Genet. 91:15-26(2012).
CC -!- FUNCTION: May function as a calcium/proton transporter involved in
CC calcium and in lysosomal pH homeostasis. Therefore, it may play an
CC indirect role in protein glycosylation. {ECO:0000269|PubMed:22683087,
CC ECO:0000269|PubMed:23569283}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi
CC network membrane. Lysosome membrane. Early endosome membrane. Late
CC endosome membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC07-2; Sequence=VSP_056691;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:22683087}.
CC -!- DISEASE: Congenital disorder of glycosylation 2K (CDG2K) [MIM:614727]:
CC An autosomal recessive disorder with a variable phenotype. Affected
CC individuals show psychomotor retardation and growth retardation, and
CC most have short stature. Other features include dysmorphism, hypotonia,
CC eye abnormalities, acquired microcephaly, hepatomegaly, and skeletal
CC dysplasia. Congenital disorders of glycosylation are caused by a defect
CC in glycoprotein biosynthesis and characterized by under-glycosylated
CC serum glycoproteins and a wide variety of clinical features. The broad
CC spectrum of features reflects the critical role of N-glycoproteins
CC during embryonic development, differentiation, and maintenance of cell
CC functions. {ECO:0000269|PubMed:22683087, ECO:0000269|PubMed:23430531,
CC ECO:0000269|PubMed:23575229}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GDT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67653.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132746; AAL75947.1; -; mRNA.
DR EMBL; AF183409; AAG09678.1; -; mRNA.
DR EMBL; AF220188; AAF67653.1; ALT_FRAME; mRNA.
DR EMBL; AK290663; BAF83352.1; -; mRNA.
DR EMBL; AK295289; BAG58273.1; -; mRNA.
DR EMBL; AC069200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05467.1; -; Genomic_DNA.
DR EMBL; BC003545; AAH03545.2; -; mRNA.
DR EMBL; BC104980; AAI04981.1; -; mRNA.
DR EMBL; BC104978; AAI04979.1; -; mRNA.
DR EMBL; BC107582; AAI07583.1; -; mRNA.
DR CCDS; CCDS3499.1; -. [Q9HC07-1]
DR RefSeq; NP_060945.2; NM_018475.4. [Q9HC07-1]
DR RefSeq; XP_016863901.1; XM_017008412.1. [Q9HC07-2]
DR AlphaFoldDB; Q9HC07; -.
DR BioGRID; 120960; 98.
DR IntAct; Q9HC07; 47.
DR MINT; Q9HC07; -.
DR STRING; 9606.ENSP00000370736; -.
DR TCDB; 2.A.106.2.2; the ca(2+):h(+) antiporter-2 (caca2) family.
DR GlyGen; Q9HC07; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HC07; -.
DR MetOSite; Q9HC07; -.
DR PhosphoSitePlus; Q9HC07; -.
DR SwissPalm; Q9HC07; -.
DR BioMuta; TMEM165; -.
DR DMDM; 74718825; -.
DR EPD; Q9HC07; -.
DR jPOST; Q9HC07; -.
DR MassIVE; Q9HC07; -.
DR MaxQB; Q9HC07; -.
DR PaxDb; Q9HC07; -.
DR PeptideAtlas; Q9HC07; -.
DR PRIDE; Q9HC07; -.
DR ProteomicsDB; 4251; -.
DR ProteomicsDB; 81617; -. [Q9HC07-1]
DR Antibodypedia; 44090; 128 antibodies from 21 providers.
DR DNASU; 55858; -.
DR Ensembl; ENST00000381334.10; ENSP00000370736.5; ENSG00000134851.13. [Q9HC07-1]
DR GeneID; 55858; -.
DR KEGG; hsa:55858; -.
DR MANE-Select; ENST00000381334.10; ENSP00000370736.5; NM_018475.5; NP_060945.2.
DR UCSC; uc003hax.4; human. [Q9HC07-1]
DR CTD; 55858; -.
DR DisGeNET; 55858; -.
DR GeneCards; TMEM165; -.
DR GeneReviews; TMEM165; -.
DR HGNC; HGNC:30760; TMEM165.
DR HPA; ENSG00000134851; Low tissue specificity.
DR MalaCards; TMEM165; -.
DR MIM; 614726; gene.
DR MIM; 614727; phenotype.
DR neXtProt; NX_Q9HC07; -.
DR OpenTargets; ENSG00000134851; -.
DR Orphanet; 314667; TMEM165-CDG.
DR PharmGKB; PA147357214; -.
DR VEuPathDB; HostDB:ENSG00000134851; -.
DR eggNOG; KOG2881; Eukaryota.
DR GeneTree; ENSGT00390000005261; -.
DR HOGENOM; CLU_040186_0_1_1; -.
DR InParanoid; Q9HC07; -.
DR OMA; QGKWHSF; -.
DR OrthoDB; 919566at2759; -.
DR PhylomeDB; Q9HC07; -.
DR TreeFam; TF105960; -.
DR PathwayCommons; Q9HC07; -.
DR SignaLink; Q9HC07; -.
DR BioGRID-ORCS; 55858; 96 hits in 1093 CRISPR screens.
DR ChiTaRS; TMEM165; human.
DR GenomeRNAi; 55858; -.
DR Pharos; Q9HC07; Tbio.
DR PRO; PR:Q9HC07; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9HC07; protein.
DR Bgee; ENSG00000134851; Expressed in corpus callosum and 194 other tissues.
DR ExpressionAtlas; Q9HC07; baseline and differential.
DR Genevisible; Q9HC07; HS.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:UniProtKB.
DR GO; GO:0032468; P:Golgi calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0032472; P:Golgi calcium ion transport; IDA:UniProtKB.
DR GO; GO:0071421; P:manganese ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; IMP:UniProtKB.
DR InterPro; IPR001727; Gdt1.
DR PANTHER; PTHR12608; PTHR12608; 1.
DR Pfam; PF01169; UPF0016; 2.
DR PROSITE; PS01214; UPF0016; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Congenital disorder of glycosylation;
KW Disease variant; Endosome; Golgi apparatus; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..324
FT /note="Transmembrane protein 165"
FT /id="PRO_0000247334"
FT TOPO_DOM 34..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..267
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 35..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..211
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..69
FT /note="MAAAAPGNGRASAPRLLLLFLVPLLWAPAAVRAGPDEDLSHRNKEPPAPAQQ
FT LQPQPVAVQGPEPARVE -> MEIPMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056691"
FT VARIANT 126
FT /note="R -> C (in CDG2K; alters subcellular location;
FT dbSNP:rs387907222)"
FT /evidence="ECO:0000269|PubMed:22683087,
FT ECO:0000269|PubMed:23575229"
FT /id="VAR_068446"
FT VARIANT 126
FT /note="R -> H (in CDG2K; alters subcellular location;
FT dbSNP:rs387907221)"
FT /evidence="ECO:0000269|PubMed:22683087,
FT ECO:0000269|PubMed:23575229"
FT /id="VAR_068447"
FT VARIANT 304
FT /note="G -> R (in CDG2K; accumulates in Golgi compartment;
FT dbSNP:rs886037631)"
FT /evidence="ECO:0000269|PubMed:22683087,
FT ECO:0000269|PubMed:23575229"
FT /id="VAR_068448"
FT MUTAGEN 124
FT /note="Y->S: Alters subcellular location."
FT /evidence="ECO:0000269|PubMed:23575229"
FT MUTAGEN 127
FT /note="L->G: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:23575229"
FT MUTAGEN 209..210
FT /note="LL->GG: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:23575229"
SQ SEQUENCE 324 AA; 34906 MW; A0E6C8BBFF189D72 CRC64;
MAAAAPGNGR ASAPRLLLLF LVPLLWAPAA VRAGPDEDLS HRNKEPPAPA QQLQPQPVAV
QGPEPARVEK IFTPAAPVHT NKEDPATQTN LGFIHAFVAA ISVIIVSELG DKTFFIAAIM
AMRYNRLTVL AGAMLALGLM TCLSVLFGYA TTVIPRVYTY YVSTVLFAIF GIRMLREGLK
MSPDEGQEEL EEVQAELKKK DEEFQRTKLL NGPGDVETGT SITVPQKKWL HFISPIFVQA
LTLTFLAEWG DRSQLTTIVL AAREDPYGVA VGGTVGHCLC TGLAVIGGRM IAQKISVRTV
TIIGGIVFLA FAFSALFISP DSGF
