SARAF_HUMAN
ID SARAF_HUMAN Reviewed; 339 AA.
AC Q96BY9; B3KQQ4; B7Z9J1; D3DSU7; H9MHJ8; H9MHJ9; Q53HE8; Q9UNZ3; Q9Y683;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Store-operated calcium entry-associated regulatory factor;
DE Short=SARAF;
DE Short=SOCE-associated regulatory factor;
DE AltName: Full=HBV X-transactivated gene 3 protein;
DE AltName: Full=HBV XAg-transactivated protein 3;
DE AltName: Full=Protein FOAP-7;
DE AltName: Full=Transmembrane protein 66;
DE Flags: Precursor;
GN Name=SARAF; Synonyms=TMEM66, XTP3;
GN ORFNames=HSPC035, NPD003, PSEC0019, UNQ1967/PRO4499;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, INTERACTION WITH STIM1, AND MUTAGENESIS OF GLU-148.
RC TISSUE=Heart;
RX PubMed=22464749; DOI=10.1016/j.cell.2012.01.055;
RA Palty R., Raveh A., Kaminsky I., Meller R., Reuveny E.;
RT "SARAF inactivates the store operated calcium entry machinery to prevent
RT excess calcium refilling.";
RL Cell 149:425-438(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RA Fujii Y., Tsuritani K., Yajima Y., Amemiya T., Ukai Y., Naito K.,
RA Kawaguchi A., Takayama K.;
RT "Molecular cloning of a human novel gene, FOAP-7, which are highly
RT expressed in macrophages.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 3 transactivated by hepatitis B
RT virus X antigen.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [10]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-339 (ISOFORM 1).
RC TISSUE=Pituitary;
RA Huang Q.-H., Zhou J., Song H., Peng J., Zhang Q.-H., Fu G., Dai M., Mao Y.,
RA Mao M., Chen Z., Chen J.;
RT "Human NPD003 mRNA, complete cds.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP PROTEIN SEQUENCE OF 31-45.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [14]
RP INTERACTION WITH STIM1.
RX PubMed=30481768; DOI=10.1159/000495494;
RA Albarran L., Lopez J.J., Jardin I., Sanchez-Collado J., Berna-Erro A.,
RA Smani T., Camello P.J., Salido G.M., Rosado J.A.;
RT "EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-SARAF
RT Interaction.";
RL Cell. Physiol. Biochem. 51:1164-1178(2018).
CC -!- FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE)
CC involved in protecting cells from Ca(2+) overfilling. In response to
CC cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+)
CC refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-
CC dependent SOCE activity: possibly act by facilitating the
CC deoligomerization of STIM to efficiently turn off ORAI when the
CC endoplasmic reticulum lumen is filled with the appropriate Ca(2+)
CC levels, and thus preventing the overload of the cell with excessive
CC Ca(2+) ions. {ECO:0000269|PubMed:22464749}.
CC -!- SUBUNIT: Interacts with STIM1; the interaction is inhibit by th
CC interaction of STIM1 with EFHB. {ECO:0000269|PubMed:22464749,
CC ECO:0000269|PubMed:30481768}.
CC -!- INTERACTION:
CC Q96BY9; Q13586: STIM1; NbExp=4; IntAct=EBI-722561, EBI-448878;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22464749}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:22464749}. Note=Translocates to the endoplasmic
CC reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner
CC following cytosolic Ca(2+) elevation.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BY9-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q96BY9-2; Sequence=VSP_043773;
CC -!- TISSUE SPECIFICITY: Highly expressed in macrophages.
CC {ECO:0000269|Ref.2}.
CC -!- DOMAIN: The cytoplasmic C-terminal region mediates interaction with
CC STIM1, while the N-terminal lumenal region mediates regulation of SOCE
CC activity. {ECO:0000269|PubMed:22464749}.
CC -!- SIMILARITY: Belongs to the SARAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD44487.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; JQ348891; AEZ06361.1; -; mRNA.
DR EMBL; JQ348892; AEZ06362.1; -; mRNA.
DR EMBL; AB028926; BAB82465.1; -; mRNA.
DR EMBL; AF490252; AAO85460.1; -; mRNA.
DR EMBL; AF100748; AAD43012.1; -; mRNA.
DR EMBL; AY359104; AAQ89462.1; -; mRNA.
DR EMBL; AK075340; BAG52116.1; -; mRNA.
DR EMBL; AK315956; BAH14327.1; -; mRNA.
DR EMBL; AK222632; BAD96352.1; -; mRNA.
DR EMBL; AC044849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63471.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63472.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63474.1; -; Genomic_DNA.
DR EMBL; BC015012; AAH15012.1; -; mRNA.
DR EMBL; AF078855; AAD44487.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6074.1; -. [Q96BY9-1]
DR CCDS; CCDS64866.1; -. [Q96BY9-2]
DR RefSeq; NP_001271168.1; NM_001284239.1. [Q96BY9-2]
DR RefSeq; NP_057211.4; NM_016127.5. [Q96BY9-1]
DR PDB; 6O2U; X-ray; 1.80 A; A/B=30-164.
DR PDB; 6O2V; X-ray; 1.58 A; A/B=30-164.
DR PDB; 6O2W; X-ray; 2.10 A; A/B=30-164.
DR PDBsum; 6O2U; -.
DR PDBsum; 6O2V; -.
DR PDBsum; 6O2W; -.
DR AlphaFoldDB; Q96BY9; -.
DR SMR; Q96BY9; -.
DR BioGRID; 119672; 224.
DR IntAct; Q96BY9; 40.
DR MINT; Q96BY9; -.
DR STRING; 9606.ENSP00000256255; -.
DR TCDB; 8.A.111.1.1; the store-operated ca2+ entry-associated regulatory factor (saraf) family.
DR iPTMnet; Q96BY9; -.
DR PhosphoSitePlus; Q96BY9; -.
DR BioMuta; SARAF; -.
DR DMDM; 74731293; -.
DR EPD; Q96BY9; -.
DR jPOST; Q96BY9; -.
DR MassIVE; Q96BY9; -.
DR MaxQB; Q96BY9; -.
DR PaxDb; Q96BY9; -.
DR PeptideAtlas; Q96BY9; -.
DR PRIDE; Q96BY9; -.
DR ProteomicsDB; 76130; -. [Q96BY9-1]
DR ProteomicsDB; 76131; -. [Q96BY9-2]
DR Antibodypedia; 23198; 115 antibodies from 17 providers.
DR DNASU; 51669; -.
DR Ensembl; ENST00000256255.11; ENSP00000256255.6; ENSG00000133872.14. [Q96BY9-1]
DR Ensembl; ENST00000545648.2; ENSP00000441351.1; ENSG00000133872.14. [Q96BY9-2]
DR GeneID; 51669; -.
DR KEGG; hsa:51669; -.
DR MANE-Select; ENST00000256255.11; ENSP00000256255.6; NM_016127.6; NP_057211.4.
DR UCSC; uc003xhs.5; human. [Q96BY9-1]
DR CTD; 51669; -.
DR DisGeNET; 51669; -.
DR GeneCards; SARAF; -.
DR HGNC; HGNC:28789; SARAF.
DR HPA; ENSG00000133872; Low tissue specificity.
DR MIM; 614768; gene.
DR neXtProt; NX_Q96BY9; -.
DR OpenTargets; ENSG00000133872; -.
DR PharmGKB; PA142670779; -.
DR VEuPathDB; HostDB:ENSG00000133872; -.
DR eggNOG; ENOG502QT6Y; Eukaryota.
DR GeneTree; ENSGT00390000013419; -.
DR HOGENOM; CLU_046802_0_1_1; -.
DR InParanoid; Q96BY9; -.
DR OMA; DKWVLKG; -.
DR OrthoDB; 1402326at2759; -.
DR PhylomeDB; Q96BY9; -.
DR TreeFam; TF314811; -.
DR PathwayCommons; Q96BY9; -.
DR SignaLink; Q96BY9; -.
DR BioGRID-ORCS; 51669; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; SARAF; human.
DR GeneWiki; TMEM66; -.
DR GenomeRNAi; 51669; -.
DR Pharos; Q96BY9; Tbio.
DR PRO; PR:Q96BY9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96BY9; protein.
DR Bgee; ENSG00000133872; Expressed in germinal epithelium of ovary and 211 other tissues.
DR ExpressionAtlas; Q96BY9; baseline and differential.
DR Genevisible; Q96BY9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IDA:UniProtKB.
DR InterPro; IPR009567; SARAF.
DR PANTHER; PTHR15929; PTHR15929; 1.
DR Pfam; PF06682; SARAF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium transport;
KW Direct protein sequencing; Endoplasmic reticulum; Ion transport; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 31..339
FT /note="Store-operated calcium entry-associated regulatory
FT factor"
FT /id="PRO_0000045485"
FT TOPO_DOM 31..173
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 318..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:22464749"
FT /id="VSP_043773"
FT VARIANT 78
FT /note="P -> T (in dbSNP:rs11538828)"
FT /id="VAR_054042"
FT MUTAGEN 148
FT /note="E->A: Dominant-negative mutant; leading to impair
FT inhibition of SOCE."
FT /evidence="ECO:0000269|PubMed:22464749"
FT CONFLICT 57..58
FT /note="RL -> SW (in Ref. 3; AAO85460 and 4; AAD43012)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> K (in Ref. 12; AAD44487)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> E (in Ref. 6; BAG52116)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> G (in Ref. 8; BAD96352)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="L -> S (in Ref. 8; BAD96352)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6O2V"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6O2U"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6O2V"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6O2V"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6O2V"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6O2V"
SQ SEQUENCE 339 AA; 36975 MW; 83CC0517AB635FE9 CRC64;
MAAACGPGAA GYCLLLGLHL FLLTAGPALG WNDPDRMLLR DVKALTLHYD RYTTSRRLDP
IPQLKCVGGT AGCDSYTPKV IQCQNKGWDG YDVQWECKTD LDIAYKFGKT VVSCEGYESS
EDQYVLRGSC GLEYNLDYTE LGLQKLKESG KQHGFASFSD YYYKWSSADS CNMSGLITIV
VLLGIAFVVY KLFLSDGQYS PPPYSEYPPF SHRYQRFTNS AGPPPPGFKS EFTGPQNTGH
GATSGFGSAF TGQQGYENSG PGFWTGLGTG GILGYLFGSN RAATPFSDSW YYPSYPPSYP
GTWNRAYSPL HGGSGSYSVC SNSDTKTRTA SGYGGTRRR
