AP1S1_HUMAN
ID AP1S1_HUMAN Reviewed; 158 AA.
AC P61966; B2R5D8; P82267; Q00382; Q53YA7; Q9BTN4; Q9UDW9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=AP-1 complex subunit sigma-1A;
DE AltName: Full=Adaptor protein complex AP-1 subunit sigma-1A;
DE AltName: Full=Adaptor-related protein complex 1 subunit sigma-1A;
DE AltName: Full=Clathrin assembly protein complex 1 sigma-1A small chain;
DE AltName: Full=Clathrin coat assembly protein AP19;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin sigma-1A subunit;
DE AltName: Full=HA1 19 kDa subunit;
DE AltName: Full=Sigma 1a subunit of AP-1 clathrin;
DE AltName: Full=Sigma-adaptin 1A;
DE AltName: Full=Sigma1A-adaptin;
GN Name=AP1S1; Synonyms=AP19, CLAPS1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693;
RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.;
RT "Identification and characterization of novel clathrin adaptor-related
RT proteins.";
RL J. Biol. Chem. 273:24693-24700(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [7]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP INVOLVEMENT IN MEDNIK.
RX PubMed=19057675; DOI=10.1371/journal.pgen.1000296;
RA Montpetit A., Cote S., Brustein E., Drouin C.A., Lapointe L., Boudreau M.,
RA Meloche C., Drouin R., Hudson T.J., Drapeau P., Cossette P.;
RT "Disruption of AP1S1, causing a novel neurocutaneous syndrome, perturbs
RT development of the skin and spinal cord.";
RL PLoS Genet. 4:E1000296-E1000296(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules.
CC {ECO:0000269|PubMed:9733768}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).
CC -!- INTERACTION:
CC P61966-2; P16284: PECAM1; NbExp=3; IntAct=EBI-12067760, EBI-716404;
CC P61966-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12067760, EBI-79165;
CC P61966-2; P37173: TGFBR2; NbExp=3; IntAct=EBI-12067760, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:9733768}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9733768}; Cytoplasmic side
CC {ECO:0000269|PubMed:9733768}. Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:9733768}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61966-1, Q00382-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P61966-2, Q00382-2;
CC Sequence=VSP_000171;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9733768}.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection.
CC {ECO:0000269|PubMed:16548883}.
CC -!- DISEASE: Intellectual disability, enteropathy, deafness, peripheral
CC neuropathy, ichthyosis, and keratoderma (MEDNIK) [MIM:609313]: A
CC disorder characterized by erythematous skin lesions and hyperkeratosis,
CC severe psychomotor retardation, peripheral neuropathy, sensorineural
CC hearing loss, together with elevated very-long-chain fatty acids and
CC severe congenital diarrhea. {ECO:0000269|PubMed:19057675}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45829.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB015319; BAA33391.1; -; mRNA.
DR EMBL; BT006779; AAP35425.1; -; mRNA.
DR EMBL; AK312151; BAG35085.1; -; mRNA.
DR EMBL; AC004876; AAD45829.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471197; EAW50199.1; -; Genomic_DNA.
DR EMBL; BC003561; AAH03561.1; -; mRNA.
DR CCDS; CCDS47669.1; -.
DR RefSeq; NP_001274.1; NM_001283.3. [P61966-1]
DR PDB; 4P6Z; X-ray; 3.00 A; S=1-158.
DR PDBsum; 4P6Z; -.
DR AlphaFoldDB; P61966; -.
DR SMR; P61966; -.
DR BioGRID; 107588; 38.
DR ComplexPortal; CPX-5047; Ubiquitous AP-1 Adaptor complex, sigma1a variant.
DR ComplexPortal; CPX-5050; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR CORUM; P61966; -.
DR IntAct; P61966; 11.
DR MINT; P61966; -.
DR STRING; 9606.ENSP00000336666; -.
DR TCDB; 9.B.278.1.1; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; P61966; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61966; -.
DR MetOSite; P61966; -.
DR PhosphoSitePlus; P61966; -.
DR BioMuta; AP1S1; -.
DR DMDM; 48428719; -.
DR EPD; P61966; -.
DR jPOST; P61966; -.
DR MassIVE; P61966; -.
DR MaxQB; P61966; -.
DR PaxDb; P61966; -.
DR PeptideAtlas; P61966; -.
DR PRIDE; P61966; -.
DR ProteomicsDB; 57348; -.
DR ProteomicsDB; 57349; -. [P61966-2]
DR Antibodypedia; 30972; 134 antibodies from 20 providers.
DR DNASU; 1174; -.
DR Ensembl; ENST00000337619.11; ENSP00000336666.5; ENSG00000106367.15. [P61966-1]
DR Ensembl; ENST00000443943.5; ENSP00000410780.1; ENSG00000106367.15. [P61966-1]
DR GeneID; 1174; -.
DR KEGG; hsa:1174; -.
DR MANE-Select; ENST00000337619.11; ENSP00000336666.5; NM_001283.5; NP_001274.1.
DR UCSC; uc003uxv.5; human.
DR CTD; 1174; -.
DR DisGeNET; 1174; -.
DR GeneCards; AP1S1; -.
DR HGNC; HGNC:559; AP1S1.
DR HPA; ENSG00000106367; Low tissue specificity.
DR MalaCards; AP1S1; -.
DR MIM; 603531; gene.
DR MIM; 609313; phenotype.
DR neXtProt; NX_P61966; -.
DR OpenTargets; ENSG00000106367; -.
DR Orphanet; 171851; MEDNIK syndrome.
DR PharmGKB; PA24850; -.
DR VEuPathDB; HostDB:ENSG00000106367; -.
DR eggNOG; KOG0934; Eukaryota.
DR GeneTree; ENSGT00970000193372; -.
DR HOGENOM; CLU_061221_1_3_1; -.
DR InParanoid; P61966; -.
DR OMA; MIHFFIL; -.
DR PhylomeDB; P61966; -.
DR TreeFam; TF312921; -.
DR PathwayCommons; P61966; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; P61966; -.
DR SIGNOR; P61966; -.
DR BioGRID-ORCS; 1174; 25 hits in 1077 CRISPR screens.
DR ChiTaRS; AP1S1; human.
DR GeneWiki; AP1S1; -.
DR GenomeRNAi; 1174; -.
DR Pharos; P61966; Tbio.
DR PRO; PR:P61966; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P61966; protein.
DR Bgee; ENSG00000106367; Expressed in cortical plate and 173 other tissues.
DR ExpressionAtlas; P61966; baseline and differential.
DR Genevisible; P61966; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; TAS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd14831; AP1_sigma; 1.
DR InterPro; IPR044733; AP1_sigma.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11753; PTHR11753; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Cytoplasmic vesicle;
KW Deafness; Golgi apparatus; Ichthyosis; Intellectual disability; Membrane;
KW Neuropathy; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..158
FT /note="AP-1 complex subunit sigma-1A"
FT /id="PRO_0000193797"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 128..158
FT /note="KKSVLKAIEQADLLQEEDESPRSVLEEMGLA -> TFPFSH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_000171"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 128..146
FT /evidence="ECO:0007829|PDB:4P6Z"
SQ SEQUENCE 158 AA; 18733 MW; E461937790406D8B CRC64;
MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL EWRDLKVVYK
RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE LDIIFNFEKA YFILDEFLMG
GDVQDTSKKS VLKAIEQADL LQEEDESPRS VLEEMGLA
