ID   ARL8A_HUMAN             Reviewed;         186 AA.
AC   Q96BM9; B3KXD0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   28-JAN-2026, entry version 195.
DE   RecName: Full=ADP-ribosylation factor-like protein 8A;
DE   AltName: Full=ADP-ribosylation factor-like protein 10B;
DE   AltName: Full=Novel small G protein indispensable for equal chromosome segregation 2;
GN   Name=ARL8A; Synonyms=ARL10B, GIE2;
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 TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=15331635; DOI=10.1242/jcs.01347;
RA   Okai T., Araki Y., Tada M., Tateno T., Kontani K., Katada T.;
RT   "Novel small GTPase subfamily capable of associating with tubulin is
RT   required for chromosome segregation.";
RL   J. Cell Sci. 117:4705-4715(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16537643; DOI=10.1242/jcs.02958;
RA   Hofmann I., Munro S.;
RT   "An N-terminally acetylated Arf-like GTPase is localised to lysosomes and
RT   affects their motility.";
RL   J. Cell Sci. 119:1494-1503(2006).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
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   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   [10]
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   [11]
RP   INTERACTION WITH PLEKHM1.
RX   PubMed=28325809; DOI=10.1083/jcb.201607085;
RA   Marwaha R., Arya S.B., Jagga D., Kaur H., Tuli A., Sharma M.;
RT   "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to
RT   lysosomes.";
RL   J. Cell Biol. 216:1051-1070(2017).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-186 IN COMPLEX WITH GTP ANALOG.
RG   Structural genomics consortium (SGC);
RT   "Structure of human ADP-ribosylation factor-like 10B.";
RL   Submitted (MAY-2005) to the PDB data bank.
RN   [13]
RP   INTERACTION WITH RUFY3 AND RUFY4.
RX   PubMed=35314674; DOI=10.1038/s41467-022-28952-y;
RA   Keren-Kaplan T., Saric A., Ghosh S., Williamson C.D., Jia R., Li Y.,
RA   Bonifacino J.S.;
RT   "RUFY3 and RUFY4 are ARL8 effectors that promote coupling of endolysosomes
RT   to dynein-dynactin.";
RL   Nat. Commun. 13:1506-1506(2022).
CC   -!- FUNCTION: Plays a role in lysosome motility (By similarity). In
CC       neurons, mediates the anterograde axonal long-range transport of
CC       presynaptic lysosome-related vesicles required for presynaptic
CC       biogenesis and synaptic function (By similarity). May play a role in
CC       chromosome segregation (By similarity). {ECO:0000250|UniProtKB:Q9CQW2,
CC       ECO:0000250|UniProtKB:Q9NVJ2}.
CC   -!- SUBUNIT: Interacts with PLEKHM1 (PubMed:28325809). When GTP-bound,
CC       interacts with RUFY3 and RUFY4, but not with RUFY1, nor RUFY2
CC       (PubMed:35314674). {ECO:0000269|PubMed:28325809,
CC       ECO:0000269|PubMed:35314674}.
CC   -!- INTERACTION:
CC       Q96BM9; Q96EN8: MOCOS; NbExp=4; IntAct=EBI-4401082, EBI-1220583;
CC       Q96BM9; Q9Y4G2: PLEKHM1; NbExp=2; IntAct=EBI-4401082, EBI-473814;
CC       Q96BM9; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-4401082, EBI-1053259;
CC       Q96BM9; Q13573: SNW1; NbExp=2; IntAct=EBI-4401082, EBI-632715;
CC       Q96BM9; Q9NZD8: SPG21; NbExp=5; IntAct=EBI-4401082, EBI-742688;
CC       Q96BM9; P07919: UQCRH; NbExp=6; IntAct=EBI-4401082, EBI-1224427;
CC       Q96BM9; PRO_0000041224 [Q86500]; Xeno; NbExp=2; IntAct=EBI-4401082, EBI-11478518;
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9NVJ2}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q9CQW2}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q9NVJ2}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9CQW2}. Synapse {ECO:0000250|UniProtKB:Q9CQW2}.
CC       Note=Localizes with microtubules at the spindle mid-zone during
CC       mitosis. {ECO:0000250|UniProtKB:Q9NVJ2}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:15331635}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AB118752; BAD23993.1; -; mRNA.
DR   EMBL; AK127138; BAG54442.1; -; mRNA.
DR   EMBL; AL592300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91395.1; -; Genomic_DNA.
DR   EMBL; BC015408; AAH15408.1; -; mRNA.
DR   CCDS; CCDS1421.1; -.
DR   RefSeq; NP_001243058.1; NM_001256129.1.
DR   RefSeq; NP_620150.1; NM_138795.4.
DR   PDB; 1ZD9; X-ray; 1.70 A; A=18-186.
DR   PDB; 2H18; X-ray; 1.90 A; A=9-182.
DR   PDB; 4ILE; X-ray; 2.68 A; A=1-181.
DR   PDBsum; 1ZD9; -.
DR   PDBsum; 2H18; -.
DR   PDBsum; 4ILE; -.
DR   AlphaFoldDB; Q96BM9; -.
DR   SMR; Q96BM9; -.
DR   BioGRID; 126084; 109.
DR   FunCoup; Q96BM9; 1262.
DR   IntAct; Q96BM9; 75.
DR   MINT; Q96BM9; -.
DR   STRING; 9606.ENSP00000272217; -.
DR   GlyCosmos; Q96BM9; 1 site, 1 glycan.
DR   GlyGen; Q96BM9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96BM9; -.
DR   PhosphoSitePlus; Q96BM9; -.
DR   BioMuta; ARL8A; -.
DR   DMDM; 74751775; -.
DR   jPOST; Q96BM9; -.
DR   MassIVE; Q96BM9; -.
DR   PaxDb; 9606-ENSP00000272217; -.
DR   PeptideAtlas; Q96BM9; -.
DR   ProteomicsDB; 76090; -.
DR   Pumba; Q96BM9; -.
DR   Antibodypedia; 34522; 223 antibodies from 23 providers.
DR   DNASU; 127829; -.
DR   Ensembl; ENST00000272217.7; ENSP00000272217.2; ENSG00000143862.9.
DR   GeneID; 127829; -.
DR   KEGG; hsa:127829; -.
DR   MANE-Select; ENST00000272217.7; ENSP00000272217.2; NM_138795.4; NP_620150.1.
DR   UCSC; uc001gxk.3; human.
DR   AGR; HGNC:25192; -.
DR   ClinPGx; PA134905021; -.
DR   CTD; 127829; -.
DR   DisGeNET; 127829; -.
DR   GeneCards; ARL8A; -.
DR   HGNC; HGNC:25192; ARL8A.
DR   HPA; ENSG00000143862; Tissue enhanced (brain).
DR   MIM; 616597; gene.
DR   OpenTargets; ENSG00000143862; -.
DR   VEuPathDB; HostDB:ENSG00000143862; -.
DR   eggNOG; KOG0075; Eukaryota.
DR   GeneTree; ENSGT00940000159657; -.
DR   HOGENOM; CLU_040729_10_0_1; -.
DR   InParanoid; Q96BM9; -.
DR   OMA; RFRSEWG; -.
DR   OrthoDB; 2011769at2759; -.
DR   PAN-GO; Q96BM9; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q96BM9; -.
DR   PathwayCommons; Q96BM9; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q96BM9; -.
DR   Agora; ENSG00000143862; -.
DR   BioGRID-ORCS; 127829; 17 hits in 1170 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; ARL8A; human.
DR   EvolutionaryTrace; Q96BM9; -.
DR   GeneWiki; ARL8A; -.
DR   GenomeRNAi; 127829; -.
DR   Pharos; Q96BM9; Tbio.
DR   PRO; PR:Q96BM9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96BM9; protein.
DR   Bgee; ENSG00000143862; Expressed in cortical plate and 171 other cell types or tissues.
DR   ExpressionAtlas; Q96BM9; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd04159; Arl10_like; 1.
DR   FunFam; 3.40.50.300:FF:000247; ADP-ribosylation factor-like GTPase 8A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR044154; Arl8a/8b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR45732; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 8; 1.
DR   PANTHER; PTHR45732:SF4; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 8A; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell projection;
KW   Chromosome partition; Cytoplasm; Cytoskeleton; Endosome; GTP-binding;
KW   Lysosome; Membrane; Mitosis; Nucleotide-binding; Protein transport;
KW   Proteomics identification; Reference proteome; Synapse; Transport.
FT   CHAIN           1..186
FT                   /note="ADP-ribosylation factor-like protein 8A"
FT                   /id="PRO_0000232916"
FT   INTRAMEM        1..19
FT                   /note="Note=Mediates targeting to membranes"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   HELIX           9..17
FT                   /evidence="ECO:0007829|PDB:2H18"
FT   STRAND          19..26
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           33..42
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:2H18"
FT   STRAND          54..62
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           76..79
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           82..86
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   TURN            164..166
FT                   /evidence="ECO:0007829|PDB:1ZD9"
FT   HELIX           170..179
FT                   /evidence="ECO:0007829|PDB:1ZD9"
SQ   SEQUENCE   186 AA;  21416 MW;  EE5141235CE0F414 CRC64;
     MIALFNKLLD WFKALFWKEE MELTLVGLQY SGKTTFVNVI ASGQFNEDMI PTVGFNMRKI
     TKGNVTIKLW DIGGQPRFRS MWERYCRGVS AIVYMVDAAD QEKIEASKNE LHNLLDKPQL
     QGIPVLVLGN KRDLPGALDE KELIEKMNLS AIQDREICCY SISCKEKDNI DITLQWLIQH
     SKSRRS
//