CAMLG_HUMAN
ID CAMLG_HUMAN Reviewed; 296 AA.
AC P49069; A1L3Y3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Guided entry of tail-anchored proteins factor CAMLG {ECO:0000305};
DE AltName: Full=Calcium signal-modulating cyclophilin ligand {ECO:0000312|HGNC:HGNC:1471};
GN Name=CAMLG {ECO:0000312|HGNC:HGNC:1471};
GN Synonyms=CAML {ECO:0000303|PubMed:24392163, ECO:0000312|HGNC:HGNC:1471},
GN GET2 {ECO:0000312|HGNC:HGNC:1471};
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], AND FUNCTION.
RX PubMed=7522304; DOI=10.1038/371355a0;
RA Bram R.J., Crabtree G.R.;
RT "Calcium signalling in T cells stimulated by a cyclophilin B-binding
RT protein.";
RL Nature 371:355-358(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 49-296.
RC TISSUE=Colon adenocarcinoma;
RA Morales V.M., Blumberg R.S.;
RT "An immature transcript of the CAMLG gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH TNFRSF13B.
RX PubMed=9311921; DOI=10.1126/science.278.5335.138;
RA von Buelow G.-U., Bram R.J.;
RT "NF-AT activation induced by a CAML-interacting member of the tumor
RT necrosis factor receptor superfamily.";
RL Science 278:138-141(1997).
RN [7]
RP INTERACTION WITH HHV-8 PROTEIN K7 (MICROBIAL INFECTION).
RX PubMed=12388711; DOI=10.1128/jvi.76.22.11491-11504.2002;
RA Feng P., Park J., Lee B.S., Lee S.H., Bram R.J., Jung J.U.;
RT "Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a
RT cellular calcium-modulating cyclophilin ligand to modulate intracellular
RT calcium concentration and inhibit apoptosis.";
RL J. Virol. 76:11491-11504(2002).
RN [8]
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 [9]
RP FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF 32-ARG--LYS-35.
RX PubMed=23041287; DOI=10.1016/j.molcel.2012.08.028;
RA Yamamoto Y., Sakisaka T.;
RT "Molecular machinery for insertion of tail-anchored membrane proteins into
RT the endoplasmic reticulum membrane in mammalian cells.";
RL Mol. Cell 48:387-397(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, AND INTERACTION WITH GET1 AND GET3.
RX PubMed=24392163; DOI=10.1371/journal.pone.0085033;
RA Vilardi F., Stephan M., Clancy A., Janshoff A., Schwappach B.;
RT "WRB and CAML are necessary and sufficient to mediate tail-anchored protein
RT targeting to the ER membrane.";
RL PLoS ONE 9:e85033-e85033(2014).
RN [13]
RP FUNCTION.
RX PubMed=27226539; DOI=10.1074/jbc.m115.707752;
RA Colombo S.F., Cardani S., Maroli A., Vitiello A., Soffientini P.,
RA Crespi A., Bram R.F., Benfante R., Borgese N.;
RT "Tail-anchored protein insertion in mammals: function and reciprocal
RT interactions of the two subunits of the TRC40 receptor.";
RL J. Biol. Chem. 291:15292-15306(2016).
RN [14]
RP INTERACTION WITH GET1, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=31417168; DOI=10.1038/s41598-019-48363-2;
RA Carvalho H.J.F., Del Bondio A., Maltecca F., Colombo S.F., Borgese N.;
RT "The WRB Subunit of the Get3 Receptor is Required for the Correct
RT Integration of its Partner CAML into the ER.";
RL Sci. Rep. 9:11887-11887(2019).
RN [15]
RP FUNCTION, AND INTERACTION WITH GET1.
RX PubMed=32187542; DOI=10.1016/j.celrep.2020.02.084;
RA Inglis A.J., Page K.R., Guna A., Voorhees R.M.;
RT "Differential Modes of Orphan Subunit Recognition for the WRB/CAML
RT Complex.";
RL Cell Rep. 30:3691-3698(2020).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF THE GET COMPLEX, AND
RP DISULFIDE BOND.
RX PubMed=32910895; DOI=10.1016/j.molcel.2020.08.012;
RA McDowell M.A., Heimes M., Fiorentino F., Mehmood S., Farkas A.,
RA Coy-Vergara J., Wu D., Bolla J.R., Schmid V., Heinze R., Wild K.,
RA Flemming D., Pfeffer S., Schwappach B., Robinson C.V., Sinning I.;
RT "Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET
RT Insertase Complex.";
RL Mol. Cell 80:72-86(2020).
CC -!- FUNCTION: Required for the post-translational delivery of tail-anchored
CC (TA) proteins to the endoplasmic reticulum (PubMed:23041287,
CC PubMed:24392163, PubMed:27226539). Together with GET1/WRB, acts as a
CC membrane receptor for soluble GET3/TRC40, which recognizes and
CC selectively binds the transmembrane domain of TA proteins in the
CC cytosol (PubMed:23041287, PubMed:24392163, PubMed:27226539). Required
CC for the stability of GET1 (PubMed:32187542). Stimulates calcium
CC signaling in T cells through its involvement in elevation of
CC intracellular calcium (PubMed:7522304). Essential for the survival of
CC peripheral follicular B cells (By similarity).
CC {ECO:0000250|UniProtKB:P49070, ECO:0000269|PubMed:23041287,
CC ECO:0000269|PubMed:24392163, ECO:0000269|PubMed:27226539,
CC ECO:0000269|PubMed:32187542, ECO:0000269|PubMed:7522304}.
CC -!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which is
CC composed of GET1/WRB, CAMLG/GET2 and GET3/TRC40 (PubMed:23041287,
CC PubMed:24392163, PubMed:32910895). Within the complex, GET1 and CAMLG
CC form a heterotetramer which is stabilized by phosphatidylinositol
CC binding and which binds to the GET3 homodimer (PubMed:32910895).
CC Interacts (via C-terminus) with GET1 (PubMed:24392163, PubMed:31417168,
CC PubMed:32187542). Interacts (via N-terminus) with GET3 (By similarity).
CC GET3 shows a higher affinity for CAMLG than for GET1 (PubMed:24392163).
CC Interacts (via N-terminus) with TNFRSF13B/TACI (via C-terminus)
CC (PubMed:9311921). {ECO:0000250|UniProtKB:Q6DGG9,
CC ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:24392163,
CC ECO:0000269|PubMed:31417168, ECO:0000269|PubMed:32187542,
CC ECO:0000269|PubMed:32910895, ECO:0000269|PubMed:9311921}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 8/HHV-
CC 8 protein K7; this interaction modulates intracellular calcium
CC concentration. {ECO:0000269|PubMed:12388711}.
CC -!- INTERACTION:
CC P49069; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-1748958, EBI-10827839;
CC P49069; O95994: AGR2; NbExp=3; IntAct=EBI-1748958, EBI-712648;
CC P49069; P00533: EGFR; NbExp=3; IntAct=EBI-1748958, EBI-297353;
CC P49069; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-1748958, EBI-2834493;
CC P49069; Q9Y624: F11R; NbExp=3; IntAct=EBI-1748958, EBI-742600;
CC P49069; O00258: GET1; NbExp=3; IntAct=EBI-1748958, EBI-18908258;
CC P49069; O43681: GET3; NbExp=5; IntAct=EBI-1748958, EBI-2515857;
CC P49069; Q96GW1: HSP90B1; NbExp=3; IntAct=EBI-1748958, EBI-12885352;
CC P49069; P46695: IER3; NbExp=2; IntAct=EBI-1748958, EBI-1748945;
CC P49069; P16389: KCNA2; NbExp=3; IntAct=EBI-1748958, EBI-10210559;
CC P49069; P16389-2: KCNA2; NbExp=3; IntAct=EBI-1748958, EBI-11987131;
CC P49069; Q8WWG9: KCNE4; NbExp=3; IntAct=EBI-1748958, EBI-11750916;
CC P49069; O43561-2: LAT; NbExp=3; IntAct=EBI-1748958, EBI-8070286;
CC P49069; P80188: LCN2; NbExp=3; IntAct=EBI-1748958, EBI-11911016;
CC P49069; Q9NX40: OCIAD1; NbExp=3; IntAct=EBI-1748958, EBI-2683029;
CC P49069; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-1748958, EBI-740845;
CC P49069; O00264: PGRMC1; NbExp=3; IntAct=EBI-1748958, EBI-1045534;
CC P49069; P08F94: PKHD1; NbExp=3; IntAct=EBI-1748958, EBI-11693144;
CC P49069; P04843: RPN1; NbExp=3; IntAct=EBI-1748958, EBI-355963;
CC P49069; O95881: TXNDC12; NbExp=5; IntAct=EBI-1748958, EBI-2564581;
CC P49069; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-1748958, EBI-11957238;
CC P49069; Q7T6S2: orf7b; Xeno; NbExp=2; IntAct=EBI-1748958, EBI-25489089;
CC P49069; E9PZ36: Pkhd1; Xeno; NbExp=4; IntAct=EBI-1748958, EBI-11693075;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:31417168}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in brain, testis and
CC ovary.
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DR EMBL; U18242; AAA59420.1; -; mRNA.
DR EMBL; AK313156; BAG35974.1; -; mRNA.
DR EMBL; CH471062; EAW62243.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62244.1; -; Genomic_DNA.
DR EMBL; BC130325; AAI30326.1; -; mRNA.
DR EMBL; AF068179; AAC23596.1; -; mRNA.
DR CCDS; CCDS4178.1; -.
DR PIR; S47594; S47594.
DR RefSeq; NP_001736.1; NM_001745.3.
DR PDB; 6SO5; EM; 4.20 A; E/F=185-296.
DR PDBsum; 6SO5; -.
DR AlphaFoldDB; P49069; -.
DR SMR; P49069; -.
DR BioGRID; 107269; 134.
DR ComplexPortal; CPX-6464; GET complex.
DR CORUM; P49069; -.
DR IntAct; P49069; 41.
DR MINT; P49069; -.
DR STRING; 9606.ENSP00000297156; -.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB11693; Voclosporin.
DR TCDB; 3.A.19.1.1; the guided entry of tail anchored protein (get) family.
DR iPTMnet; P49069; -.
DR PhosphoSitePlus; P49069; -.
DR SwissPalm; P49069; -.
DR BioMuta; CAMLG; -.
DR DMDM; 1345662; -.
DR EPD; P49069; -.
DR jPOST; P49069; -.
DR MassIVE; P49069; -.
DR MaxQB; P49069; -.
DR PaxDb; P49069; -.
DR PeptideAtlas; P49069; -.
DR PRIDE; P49069; -.
DR ProteomicsDB; 55961; -.
DR Antibodypedia; 26345; 299 antibodies from 30 providers.
DR DNASU; 819; -.
DR Ensembl; ENST00000297156.4; ENSP00000297156.2; ENSG00000164615.6.
DR GeneID; 819; -.
DR KEGG; hsa:819; -.
DR MANE-Select; ENST00000297156.4; ENSP00000297156.2; NM_001745.4; NP_001736.1.
DR UCSC; uc003kzt.4; human.
DR CTD; 819; -.
DR DisGeNET; 819; -.
DR GeneCards; CAMLG; -.
DR HGNC; HGNC:1471; CAMLG.
DR HPA; ENSG00000164615; Low tissue specificity.
DR MIM; 601118; gene.
DR neXtProt; NX_P49069; -.
DR OpenTargets; ENSG00000164615; -.
DR PharmGKB; PA26053; -.
DR VEuPathDB; HostDB:ENSG00000164615; -.
DR eggNOG; ENOG502QVCE; Eukaryota.
DR GeneTree; ENSGT00390000015996; -.
DR HOGENOM; CLU_081881_0_0_1; -.
DR InParanoid; P49069; -.
DR OMA; GNAVEEF; -.
DR OrthoDB; 1203862at2759; -.
DR PhylomeDB; P49069; -.
DR TreeFam; TF331902; -.
DR PathwayCommons; P49069; -.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; P49069; -.
DR BioGRID-ORCS; 819; 241 hits in 1087 CRISPR screens.
DR ChiTaRS; CAMLG; human.
DR GeneWiki; CAMLG; -.
DR GenomeRNAi; 819; -.
DR Pharos; P49069; Tbio.
DR PRO; PR:P49069; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P49069; protein.
DR Bgee; ENSG00000164615; Expressed in secondary oocyte and 204 other tissues.
DR ExpressionAtlas; P49069; baseline and differential.
DR Genevisible; P49069; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0043529; C:GET complex; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; IC:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR016719; CAMLG.
DR PANTHER; PTHR15026; PTHR15026; 1.
DR Pfam; PF14963; Get2_like; 1.
DR PIRSF; PIRSF018259; CAML; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; ER-Golgi transport;
KW Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Guided entry of tail-anchored proteins factor CAMLG"
FT /id="PRO_0000089291"
FT TOPO_DOM 1..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31417168"
FT TRANSMEM 190..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..212
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:31417168"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31417168"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..296
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:31417168"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 208..284
FT /evidence="ECO:0000269|PubMed:32910895,
FT ECO:0007744|PDB:6SO5"
FT VARIANT 78
FT /note="V -> I (in dbSNP:rs12657663)"
FT /id="VAR_024297"
FT VARIANT 100
FT /note="G -> S (in dbSNP:rs11552197)"
FT /id="VAR_050710"
FT MUTAGEN 32..35
FT /note="RRRK->EEEE: Abolishes binding to GET3."
FT /evidence="ECO:0000269|PubMed:23041287"
SQ SEQUENCE 296 AA; 32953 MW; 22DCD8CF022FEF09 CRC64;
MESMAVATDG GERPGVPAGS GLSASQRRAE LRRRKLLMNS EQRINRIMGF HRPGSGAEEE
SQTKSKQQDS DKLNSLSVPS VSKRVVLGDS VSTGTTDQQG GVAEVKGTQL GDKLDSFIKP
PECSSDVNLE LRQRNRGDLT ADSVQRGSRH GLEQYLSRFE EAMKLRKQLI SEKPSQEDGN
TTEEFDSFRI FRLVGCALLA LGVRAFVCKY LSIFAPFLTL QLAYMGLYKY FPKSEKKIKT
TVLTAALLLS GIPAEVINRS MDTYSKMGEV FTDLCVYFFT FIFCHELLDY WGSEVP
