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EIF1A_HUMAN
ID   EIF1A_HUMAN             Reviewed;         165 AA.
AC   Q8N9N8; B2R4N5; Q9BSC1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable RNA-binding protein EIF1AD;
DE   AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein;
DE   AltName: Full=Haponin;
GN   Name=EIF1AD;
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   PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH GAPDH, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=20644585; DOI=10.1134/s1068162010030027;
RA   Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A.,
RA   Lipkin V.M.;
RT   "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase
RT   in the CHO-K1 cell line.";
RL   Bioorg. Khim. 36:312-318(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
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.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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-23.
RC   TISSUE=Skin;
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   INTERACTION WITH STAT1.
RX   PubMed=16189514; DOI=10.1038/nature04209;
RA   Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N.,
RA   Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N.,
RA   Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V.,
RA   Wong S.L., Franklin G., Li S., Albala J.S., Lim J., Fraughton C.,
RA   Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J.,
RA   Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L.,
RA   Cusick M.E., Hill D.E., Roth F.P., Vidal M.;
RT   "Towards a proteome-scale map of the human protein-protein interaction
RT   network.";
RL   Nature 437:1173-1178(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
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, AND SUBCELLULAR LOCATION.
RX   PubMed=22095125; DOI=10.1134/s1607672911050097;
RA   Smirnova E.V., Rakitina T.V., Bogatova O.V., Ivanova D.L., Vorobyeva E.E.,
RA   Lipkin A.V., Kostanyan I.A., Lipkin V.M.;
RT   "Novel protein haponin regulates cellular response to oxidative stress.";
RL   Dokl. Biochem. Biophys. 440:225-227(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, AND
RP   IDENTIFICATION BY 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   STRUCTURE BY NMR OF 16-114.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the eukaryotic initiation factor 1A in MGC11102
RT   protein.";
RL   Submitted (SEP-2006) to the PDB data bank.
CC   -!- FUNCTION: Plays a role into cellular response to oxidative stress.
CC       Decreases cell proliferation. {ECO:0000269|PubMed:20644585,
CC       ECO:0000269|PubMed:22095125}.
CC   -!- SUBUNIT: Interacts with GAPDH and STAT1. {ECO:0000269|PubMed:16189514,
CC       ECO:0000269|PubMed:20644585}.
CC   -!- INTERACTION:
CC       Q8N9N8; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-750700, EBI-297683;
CC       Q8N9N8; Q8N7W2-2: BEND7; NbExp=6; IntAct=EBI-750700, EBI-10181188;
CC       Q8N9N8; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-750700, EBI-711501;
CC       Q8N9N8; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-750700, EBI-747776;
CC       Q8N9N8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-750700, EBI-742887;
CC       Q8N9N8; O95995: GAS8; NbExp=3; IntAct=EBI-750700, EBI-1052570;
CC       Q8N9N8; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-750700, EBI-17857617;
CC       Q8N9N8; Q49A26: GLYR1; NbExp=4; IntAct=EBI-750700, EBI-2804292;
CC       Q8N9N8; Q92759: GTF2H4; NbExp=3; IntAct=EBI-750700, EBI-6380495;
CC       Q8N9N8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-750700, EBI-739832;
CC       Q8N9N8; P50222: MEOX2; NbExp=3; IntAct=EBI-750700, EBI-748397;
CC       Q8N9N8; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-750700, EBI-10172526;
CC       Q8N9N8; Q8N565: MREG; NbExp=3; IntAct=EBI-750700, EBI-10978787;
CC       Q8N9N8; P26367: PAX6; NbExp=3; IntAct=EBI-750700, EBI-747278;
CC       Q8N9N8; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-750700, EBI-10302990;
CC       Q8N9N8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-750700, EBI-79165;
CC       Q8N9N8; Q96BK5: PINX1; NbExp=3; IntAct=EBI-750700, EBI-721782;
CC       Q8N9N8; A6NK89: RASSF10; NbExp=3; IntAct=EBI-750700, EBI-6912267;
CC       Q8N9N8; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-750700, EBI-1210429;
CC       Q8N9N8; Q5RL73: RBM48; NbExp=3; IntAct=EBI-750700, EBI-473821;
CC       Q8N9N8; O00560: SDCBP; NbExp=6; IntAct=EBI-750700, EBI-727004;
CC       Q8N9N8; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-750700, EBI-742426;
CC       Q8N9N8; P42224: STAT1; NbExp=4; IntAct=EBI-750700, EBI-1057697;
CC       Q8N9N8; O75558: STX11; NbExp=6; IntAct=EBI-750700, EBI-714135;
CC       Q8N9N8; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-750700, EBI-10217641;
CC       Q8N9N8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-750700, EBI-11139477;
CC       Q8N9N8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-750700, EBI-11741437;
CC       Q8N9N8; P19237: TNNI1; NbExp=3; IntAct=EBI-750700, EBI-746692;
CC       Q8N9N8; O43829: ZBTB14; NbExp=3; IntAct=EBI-750700, EBI-10176632;
CC       Q8N9N8; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-750700, EBI-742740;
CC       Q8N9N8; P59817: ZNF280A; NbExp=3; IntAct=EBI-750700, EBI-8489342;
CC       Q8N9N8; Q96K83: ZNF521; NbExp=3; IntAct=EBI-750700, EBI-6597673;
CC       Q8N9N8; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-750700, EBI-373363;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20644585,
CC       ECO:0000269|PubMed:22095125}.
CC   -!- TISSUE SPECIFICITY: Expressed in the glioblastoma cell line U-87MG, the
CC       embryonic kidney cell line HEK293, the pancreatic carcinoma cell line
CC       PANC-1, the breast carcinoma cell line MCF-7, the lung cancer cell line
CC       NCI-H460, and the chronic myelogenous leukemia cell line K-562.
CC       {ECO:0000269|PubMed:20644585}.
CC   -!- SIMILARITY: Belongs to the EIF1AD family. {ECO:0000305}.
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DR   EMBL; AK094129; BAC04293.1; -; mRNA.
DR   EMBL; AK311891; BAG34832.1; -; mRNA.
DR   EMBL; CH471076; EAW74478.1; -; Genomic_DNA.
DR   EMBL; BC005131; AAH05131.1; -; mRNA.
DR   CCDS; CCDS8124.1; -.
DR   RefSeq; NP_001229410.1; NM_001242481.1.
DR   RefSeq; NP_001229411.1; NM_001242482.1.
DR   RefSeq; NP_001229412.1; NM_001242483.1.
DR   RefSeq; NP_001229413.1; NM_001242484.1.
DR   RefSeq; NP_001229414.1; NM_001242485.1.
DR   RefSeq; NP_001229415.1; NM_001242486.1.
DR   RefSeq; NP_115701.2; NM_032325.3.
DR   RefSeq; XP_016873901.1; XM_017018412.1.
DR   PDB; 2DGY; NMR; -; A=17-114.
DR   PDB; 6ZXF; EM; 3.70 A; j=1-165.
DR   PDB; 6ZXG; EM; 2.60 A; j=1-165.
DR   PDB; 6ZXH; EM; 2.70 A; j=1-165.
DR   PDBsum; 2DGY; -.
DR   PDBsum; 6ZXF; -.
DR   PDBsum; 6ZXG; -.
DR   PDBsum; 6ZXH; -.
DR   AlphaFoldDB; Q8N9N8; -.
DR   SMR; Q8N9N8; -.
DR   BioGRID; 124012; 89.
DR   IntAct; Q8N9N8; 38.
DR   MINT; Q8N9N8; -.
DR   STRING; 9606.ENSP00000309175; -.
DR   GlyGen; Q8N9N8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N9N8; -.
DR   PhosphoSitePlus; Q8N9N8; -.
DR   BioMuta; EIF1AD; -.
DR   DMDM; 74729733; -.
DR   EPD; Q8N9N8; -.
DR   jPOST; Q8N9N8; -.
DR   MassIVE; Q8N9N8; -.
DR   MaxQB; Q8N9N8; -.
DR   PaxDb; Q8N9N8; -.
DR   PeptideAtlas; Q8N9N8; -.
DR   PRIDE; Q8N9N8; -.
DR   ProteomicsDB; 72570; -.
DR   Antibodypedia; 44351; 77 antibodies from 13 providers.
DR   DNASU; 84285; -.
DR   Ensembl; ENST00000312234.6; ENSP00000309175.2; ENSG00000175376.9.
DR   Ensembl; ENST00000526451.5; ENSP00000436644.1; ENSG00000175376.9.
DR   Ensembl; ENST00000527249.5; ENSP00000435439.1; ENSG00000175376.9.
DR   Ensembl; ENST00000529964.5; ENSP00000435942.2; ENSG00000175376.9.
DR   Ensembl; ENST00000533544.6; ENSP00000434056.1; ENSG00000175376.9.
DR   GeneID; 84285; -.
DR   KEGG; hsa:84285; -.
DR   MANE-Select; ENST00000533544.6; ENSP00000434056.1; NM_001242481.2; NP_001229410.1.
DR   UCSC; uc001ogm.3; human.
DR   CTD; 84285; -.
DR   DisGeNET; 84285; -.
DR   GeneCards; EIF1AD; -.
DR   HGNC; HGNC:28147; EIF1AD.
DR   HPA; ENSG00000175376; Low tissue specificity.
DR   MIM; 618473; gene.
DR   neXtProt; NX_Q8N9N8; -.
DR   OpenTargets; ENSG00000175376; -.
DR   PharmGKB; PA162384553; -.
DR   VEuPathDB; HostDB:ENSG00000175376; -.
DR   eggNOG; KOG2925; Eukaryota.
DR   GeneTree; ENSGT00390000011180; -.
DR   HOGENOM; CLU_106477_2_1_1; -.
DR   InParanoid; Q8N9N8; -.
DR   OMA; YLVSMPR; -.
DR   OrthoDB; 1431625at2759; -.
DR   PhylomeDB; Q8N9N8; -.
DR   TreeFam; TF314439; -.
DR   PathwayCommons; Q8N9N8; -.
DR   SignaLink; Q8N9N8; -.
DR   BioGRID-ORCS; 84285; 608 hits in 1082 CRISPR screens.
DR   ChiTaRS; EIF1AD; human.
DR   EvolutionaryTrace; Q8N9N8; -.
DR   GenomeRNAi; 84285; -.
DR   Pharos; Q8N9N8; Tdark.
DR   PRO; PR:Q8N9N8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8N9N8; protein.
DR   Bgee; ENSG00000175376; Expressed in pancreatic ductal cell and 182 other tissues.
DR   ExpressionAtlas; Q8N9N8; baseline and differential.
DR   Genevisible; Q8N9N8; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR039294; EIF1AD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   PANTHER; PTHR21641; PTHR21641; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..165
FT                   /note="Probable RNA-binding protein EIF1AD"
FT                   /id="PRO_0000314151"
FT   DOMAIN          5..89
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00181"
FT   REGION          112..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           6..12
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           56..65
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         33
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         23
FT                   /note="D -> N (in dbSNP:rs17849919)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037851"
FT   VARIANT         159
FT                   /note="S -> N (in dbSNP:rs2276017)"
FT                   /id="VAR_037852"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          26..35
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   TURN            55..60
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          78..88
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   HELIX           92..98
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:6ZXG"
SQ   SEQUENCE   165 AA;  19053 MW;  33FB5ACB777084B2 CRC64;
     MSQATKRKHV VKEVLGEHIV PSDQQQIVRV LRTPGNNLHE VETAQGQRFL VSMPSKYRKN
     IWIKRGDFLI VDPIEEGEKV KAEISFVLCK DHVRSLQKEG FWPEAFSEVA EKHNNRNRQT
     QPELPAEPQL SGEESSSEDD SDLFVNTNRR QYHESEEESE EEEAA
 
 
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