ID RAB2A_HUMAN Reviewed; 212 AA. AC P61019; B2R5W8; B4DMQ5; P08886; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 1. DT 23-FEB-2022, entry version 174. DE RecName: Full=Ras-related protein Rab-2A; GN Name=RAB2A; Synonyms=RAB2; 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). RX PubMed=3057444; DOI=10.1093/nar/16.21.10368; RA Tachibana K., Umezawa A., Kato S., Takano T.; RT "Nucleotide sequence of a new YPT1-related human cDNA which belongs to the RT ras gene superfamily."; RL Nucleic Acids Res. 16:10368-10368(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2501306; RA Zahraoui A., Touchot N., Chardin P., Tavitian A.; RT "The human Rab genes encode a family of GTP-binding proteins related to RT yeast YPT1 and SEC4 products involved in secretion."; RL J. Biol. Chem. 264:12394-12401(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Brain cortex; 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 [6] 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 [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [9] RP ISOPRENYLATION AT CYS-211 AND CYS-212. RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264; RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., RA Balch W.E., Buss J.E., Der C.J.; RT "Isoprenoid modification of rab proteins terminating in CC or CXC motifs."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991). RN [10] RP INTERACTION WITH PRKCI. RX PubMed=14570876; DOI=10.1074/jbc.m309343200; RA Tisdale E.J.; RT "Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda RT and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate RT dehydrogenase phosphorylation."; RL J. Biol. Chem. 278:52524-52530(2003). RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] 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 [14] RP INTERACTION WITH TRIP11. RX PubMed=25473115; DOI=10.1091/mbc.e14-10-1450; RA Sato K., Roboti P., Mironov A.A., Lowe M.; RT "Coupling of vesicle tethering and Rab binding is required for in vivo RT functionality of the golgin GMAP-210."; RL Mol. Biol. Cell 26:537-553(2015). RN [15] 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 [16] RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP. RX PubMed=16034420; DOI=10.1038/nature03798; RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.; RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."; RL Nature 436:415-419(2005). CC -!- FUNCTION: Required for protein transport from the endoplasmic reticulum CC to the Golgi complex. CC -!- SUBUNIT: Interacts with PRKCI. Interacts with TRIP11 (PubMed:25473115). CC {ECO:0000269|PubMed:14570876, ECO:0000269|PubMed:16034420, CC ECO:0000269|PubMed:25473115}. CC -!- INTERACTION: CC P61019; Q9H2G9: BLZF1; NbExp=9; IntAct=EBI-752037, EBI-2548012; CC P61019; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-752037, EBI-11977221; CC P61019; Q9Y281: CFL2; NbExp=3; IntAct=EBI-752037, EBI-351218; CC P61019; Q8IWE2: FAM114A1; NbExp=7; IntAct=EBI-752037, EBI-2686288; CC P61019; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-752037, EBI-10973142; CC P61019; Q8IYT1: FAM71A; NbExp=3; IntAct=EBI-752037, EBI-20113335; CC P61019; Q8NEG0: FAM71C; NbExp=7; IntAct=EBI-752037, EBI-752049; CC P61019; Q6NXP2-2: FAM71F2; NbExp=4; IntAct=EBI-752037, EBI-12925824; CC P61019; Q8N878: FRMD1; NbExp=3; IntAct=EBI-752037, EBI-11749206; CC P61019; Q08379: GOLGA2; NbExp=7; IntAct=EBI-752037, EBI-618309; CC P61019; Q96HZ4: HES6; NbExp=3; IntAct=EBI-752037, EBI-7469266; CC P61019; Q05084: ICA1; NbExp=4; IntAct=EBI-752037, EBI-1046751; CC P61019; Q13794-2: PMAIP1; NbExp=3; IntAct=EBI-752037, EBI-12170575; CC P61019; Q96FJ0: STAMBPL1; NbExp=10; IntAct=EBI-752037, EBI-745021; CC P61019; Q3MII6: TBC1D25; NbExp=3; IntAct=EBI-752037, EBI-11899977; CC P61019; Q9BUB7: TMEM70; NbExp=3; IntAct=EBI-752037, EBI-726363; CC P61019; Q9C029: TRIM7; NbExp=3; IntAct=EBI-752037, EBI-2813981; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate CC compartment membrane {ECO:0000269|PubMed:17081065}; Lipid-anchor CC {ECO:0000269|PubMed:17081065}. Melanosome CC {ECO:0000269|PubMed:17081065}. Endoplasmic reticulum membrane CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Identified by mass CC spectrometry in melanosome fractions from stage I to stage IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P61019-1; Sequence=Displayed; CC Name=2; CC IsoId=P61019-2; Sequence=VSP_042917; CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X12953; CAA31411.1; -; mRNA. DR EMBL; M28213; AAA60241.1; -; mRNA. DR EMBL; AF498930; AAM21078.1; -; mRNA. DR EMBL; BT019695; AAV38501.1; -; mRNA. DR EMBL; AK297576; BAG59967.1; -; mRNA. DR EMBL; AK312344; BAG35265.1; -; mRNA. DR EMBL; AC068389; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079065; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471068; EAW86827.1; -; Genomic_DNA. DR EMBL; BC008929; AAH08929.1; -; mRNA. DR CCDS; CCDS56537.1; -. [P61019-2] DR CCDS; CCDS6175.1; -. [P61019-1] DR PIR; B34323; B34323. DR RefSeq; NP_001229573.1; NM_001242644.1. [P61019-2] DR RefSeq; NP_002856.1; NM_002865.2. [P61019-1] DR PDB; 1Z0A; X-ray; 2.12 A; A/B/C/D=2-170. DR PDBsum; 1Z0A; -. DR SMR; P61019; -. DR BioGRID; 111800; 501. DR DIP; DIP-316N; -. DR IntAct; P61019; 75. DR MINT; P61019; -. DR STRING; 9606.ENSP00000262646; -. DR ChEMBL; CHEMBL4105893; -. DR GlyGen; P61019; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61019; -. DR PhosphoSitePlus; P61019; -. DR SwissPalm; P61019; -. DR BioMuta; RAB2A; -. DR DMDM; 46577636; -. DR EPD; P61019; -. DR jPOST; P61019; -. DR MassIVE; P61019; -. DR MaxQB; P61019; -. DR PaxDb; P61019; -. DR PeptideAtlas; P61019; -. DR PRIDE; P61019; -. DR ProteomicsDB; 57251; -. [P61019-1] DR ProteomicsDB; 57252; -. [P61019-2] DR TopDownProteomics; P61019-1; -. [P61019-1] DR TopDownProteomics; P61019-2; -. [P61019-2] DR Antibodypedia; 4367; 337 antibodies from 37 providers. DR DNASU; 5862; -. DR Ensembl; ENST00000262646; ENSP00000262646; ENSG00000104388. DR Ensembl; ENST00000531289; ENSP00000431846; ENSG00000104388. [P61019-2] DR GeneID; 5862; -. DR KEGG; hsa:5862; -. DR MANE-Select; ENST00000262646.12; ENSP00000262646.7; NM_002865.3; NP_002856.1. DR UCSC; uc003xud.3; human. [P61019-1] DR CTD; 5862; -. DR DisGeNET; 5862; -. DR GeneCards; RAB2A; -. DR HGNC; HGNC:9763; RAB2A. DR HPA; ENSG00000104388; Low tissue specificity. DR MIM; 179509; gene. DR neXtProt; NX_P61019; -. DR OpenTargets; ENSG00000104388; -. DR PharmGKB; PA162400618; -. DR VEuPathDB; HostDB:ENSG00000104388; -. DR eggNOG; KOG0098; Eukaryota. DR GeneTree; ENSGT00940000153886; -. DR HOGENOM; CLU_041217_23_1_1; -. DR InParanoid; P61019; -. DR OMA; ANGVMQY; -. DR PhylomeDB; P61019; -. DR TreeFam; TF300032; -. DR BRENDA; 3.6.5.2; 2681. DR PathwayCommons; P61019; -. DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR SignaLink; P61019; -. DR SIGNOR; P61019; -. DR BioGRID-ORCS; 5862; 23 hits in 1056 CRISPR screens. DR ChiTaRS; RAB2A; human. DR EvolutionaryTrace; P61019; -. DR GeneWiki; RAB2A; -. DR GenomeRNAi; 5862; -. DR Pharos; P61019; Tbio. DR PRO; PR:P61019; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P61019; protein. DR Bgee; ENSG00000104388; Expressed in frontal cortex and 253 other tissues. DR ExpressionAtlas; P61019; baseline and differential. DR Genevisible; P61019; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:ProtInc. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Endoplasmic reticulum; KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..212 FT /note="Ras-related protein Rab-2A" FT /id="PRO_0000121066" FT NP_BIND 13..21 FT /note="GTP" FT /evidence="ECO:0007744|PDB:1Z0A" FT NP_BIND 61..65 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:P62820" FT NP_BIND 119..122 FT /note="GTP" FT /evidence="ECO:0007744|PDB:1Z0A" FT NP_BIND 149..151 FT /note="GTP" FT /evidence="ECO:0007744|PDB:1Z0A" FT REGION 2..19 FT /note="Required for interaction with PRKCI" FT /evidence="ECO:0000269|PubMed:14570876" FT MOTIF 35..43 FT /note="Effector region" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT LIPID 211 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736" FT LIPID 212 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736" FT VAR_SEQ 16..39 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042917" FT CONFLICT 144 FT /note="I -> M (in Ref. 2; AAA60241)" FT /evidence="ECO:0000305" FT STRAND 4..14 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 19..28 FT /evidence="ECO:0007829|PDB:1Z0A" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:1Z0A" FT STRAND 53..61 FT /evidence="ECO:0007829|PDB:1Z0A" FT TURN 66..69 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:1Z0A" FT STRAND 79..87 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:1Z0A" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 131..141 FT /evidence="ECO:0007829|PDB:1Z0A" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:1Z0A" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:1Z0A" FT HELIX 156..169 FT /evidence="ECO:0007829|PDB:1Z0A" SQ SEQUENCE 212 AA; 23546 MW; F8731E3F8FB399A3 CRC64; MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN EANGIKIGPQ HAATNATHAG NQGGQQAGGG CC //