AP2S1_HUMAN
ID AP2S1_HUMAN Reviewed; 142 AA.
AC P53680; B2R4Z4; O75977; Q6PK67;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=AP-2 complex subunit sigma;
DE AltName: Full=Adaptor protein complex AP-2 subunit sigma;
DE AltName: Full=Adaptor-related protein complex 2 subunit sigma;
DE AltName: Full=Clathrin assembly protein 2 sigma small chain;
DE AltName: Full=Clathrin coat assembly protein AP17;
DE AltName: Full=Clathrin coat-associated protein AP17;
DE AltName: Full=HA2 17 kDa subunit;
DE AltName: Full=Plasma membrane adaptor AP-2 17 kDa protein;
DE AltName: Full=Sigma2-adaptin;
GN Name=AP2S1; Synonyms=AP17, CLAPS2;
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).
RC TISSUE=Kidney;
RX PubMed=9040778; DOI=10.1159/000134463;
RA Winterpacht A., Endele S., Enklaar T., Fuhry M., Zabel B.;
RT "Human CLAPS2 encoding AP17, a small chain of the clathrin-associated
RT protein complex: cDNA cloning and chromosomal assignment to
RT 19q13.2-->q13.3.";
RL Cytogenet. Cell Genet. 75:132-135(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=9767099; DOI=10.1016/s0378-1119(98)00406-5;
RA Holzmann K., Poeltl A., Sauermann G.;
RT "A novel spliced transcript of human CLAPS2 encoding a protein alternative
RT to clathrin adaptor protein AP17.";
RL Gene 220:39-44(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
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].
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] (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 [6]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in the
RT post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [7]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX PubMed=19033387; DOI=10.1242/jcs.033522;
RA Lau A.W., Chou M.M.;
RT "The adaptor complex AP-2 regulates post-endocytic trafficking through the
RT non-clathrin Arf6-dependent endocytic pathway.";
RL J. Cell Sci. 121:4008-4017(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, 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 [10]
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 [11]
RP FUNCTION, INVOLVEMENT IN HHC3, VARIANTS HHC3 CYS-15; HIS-15 AND LEU-15, AND
RP CHARACTERIZATION OF VARIANTS HHC3 CYS-15; HIS-15 AND LEU-15.
RX PubMed=23222959; DOI=10.1038/ng.2492;
RA Nesbit M.A., Hannan F.M., Howles S.A., Reed A.A., Cranston T.,
RA Thakker C.E., Gregory L., Rimmer A.J., Rust N., Graham U., Morrison P.J.,
RA Hunter S.J., Whyte M.P., McVean G., Buck D., Thakker R.V.;
RT "Mutations in AP2S1 cause familial hypocalciuric hypercalcemia type 3.";
RL Nat. Genet. 45:93-97(2013).
RN [12]
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 [13]
RP VARIANT HHC3 LEU-15.
RX PubMed=24081735; DOI=10.1210/jc.2013-2571;
RA Fujisawa Y., Yamaguchi R., Satake E., Ohtaka K., Nakanishi T., Ozono K.,
RA Ogata T.;
RT "Identification of AP2S1 mutation and effects of low calcium formula in an
RT infant with hypercalcemia and hypercalciuria.";
RL J. Clin. Endocrinol. Metab. 98:E2022-E2027(2013).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein Transport via Transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to
CC contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By
CC similarity). May also play a role in extracellular calcium homeostasis.
CC {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838,
CC ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23222959}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1).
CC -!- INTERACTION:
CC P53680; Q6PD74: AAGAB; NbExp=8; IntAct=EBI-297662, EBI-719906;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral
CC membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded
CC from internalizing CCVs and to disengage from sites of endocytosis
CC seconds before internalization of the nascent CCV. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53680-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53680-2; Sequence=VSP_017352;
CC -!- DISEASE: Hypocalciuric hypercalcemia, familial 3 (HHC3) [MIM:600740]: A
CC form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis
CC that is transmitted as an autosomal dominant trait with a high degree
CC of penetrance. It is characterized biochemically by lifelong elevation
CC of serum calcium concentrations and is associated with inappropriately
CC low urinary calcium excretion and a normal or mildly elevated
CC circulating parathyroid hormone level. Hypermagnesemia is typically
CC present. Affected individuals are usually asymptomatic and the disorder
CC is considered benign. However, chondrocalcinosis and pancreatitis occur
CC in some adults. {ECO:0000269|PubMed:23222959,
CC ECO:0000269|PubMed:24081735}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; X97074; CAA65782.1; -; mRNA.
DR EMBL; AJ010148; CAA09018.1; -; mRNA.
DR EMBL; AJ010149; CAA09019.1; -; mRNA.
DR EMBL; AK312003; BAG34941.1; -; mRNA.
DR EMBL; CH471126; EAW57448.1; -; Genomic_DNA.
DR EMBL; BC006337; AAH06337.1; -; mRNA.
DR CCDS; CCDS12693.1; -. [P53680-2]
DR CCDS; CCDS33062.1; -. [P53680-1]
DR RefSeq; NP_001288005.1; NM_001301076.1.
DR RefSeq; NP_001288007.1; NM_001301078.1.
DR RefSeq; NP_001288010.1; NM_001301081.1.
DR RefSeq; NP_004060.2; NM_004069.4. [P53680-1]
DR RefSeq; NP_067586.1; NM_021575.3. [P53680-2]
DR PDB; 6URI; X-ray; 3.00 A; S=1-142.
DR PDBsum; 6URI; -.
DR AlphaFoldDB; P53680; -.
DR SMR; P53680; -.
DR BioGRID; 107589; 89.
DR ComplexPortal; CPX-5149; AP-2 Adaptor complex, alpha1 variant.
DR ComplexPortal; CPX-5150; AP-2 Adaptor complex, alpha2 variant.
DR IntAct; P53680; 49.
DR MINT; P53680; -.
DR STRING; 9606.ENSP00000263270; -.
DR TCDB; 9.B.278.1.4; the organellar-targeting adaptor protein complex (o-apc) family.
DR iPTMnet; P53680; -.
DR PhosphoSitePlus; P53680; -.
DR SwissPalm; P53680; -.
DR BioMuta; AP2S1; -.
DR DMDM; 51338780; -.
DR EPD; P53680; -.
DR jPOST; P53680; -.
DR MassIVE; P53680; -.
DR MaxQB; P53680; -.
DR PaxDb; P53680; -.
DR PeptideAtlas; P53680; -.
DR PRIDE; P53680; -.
DR ProteomicsDB; 56611; -. [P53680-1]
DR ProteomicsDB; 56612; -. [P53680-2]
DR TopDownProteomics; P53680-1; -. [P53680-1]
DR Antibodypedia; 31506; 166 antibodies from 26 providers.
DR DNASU; 1175; -.
DR Ensembl; ENST00000263270.11; ENSP00000263270.6; ENSG00000042753.12. [P53680-1]
DR Ensembl; ENST00000601649.1; ENSP00000470898.1; ENSG00000042753.12. [P53680-2]
DR GeneID; 1175; -.
DR KEGG; hsa:1175; -.
DR MANE-Select; ENST00000263270.11; ENSP00000263270.6; NM_004069.6; NP_004060.2.
DR UCSC; uc002pft.2; human. [P53680-1]
DR CTD; 1175; -.
DR DisGeNET; 1175; -.
DR GeneCards; AP2S1; -.
DR HGNC; HGNC:565; AP2S1.
DR HPA; ENSG00000042753; Low tissue specificity.
DR MalaCards; AP2S1; -.
DR MIM; 600740; phenotype.
DR MIM; 602242; gene.
DR neXtProt; NX_P53680; -.
DR OpenTargets; ENSG00000042753; -.
DR Orphanet; 101050; Familial hypocalciuric hypercalcemia type 3.
DR PharmGKB; PA24856; -.
DR VEuPathDB; HostDB:ENSG00000042753; -.
DR eggNOG; KOG0935; Eukaryota.
DR GeneTree; ENSGT00970000193421; -.
DR InParanoid; P53680; -.
DR OMA; IYLSHIH; -.
DR OrthoDB; 1307450at2759; -.
DR PhylomeDB; P53680; -.
DR TreeFam; TF300139; -.
DR PathwayCommons; P53680; -.
DR Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors. [P53680-1]
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-8964038; LDL clearance.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P53680; -.
DR SIGNOR; P53680; -.
DR BioGRID-ORCS; 1175; 591 hits in 1097 CRISPR screens.
DR ChiTaRS; AP2S1; human.
DR GeneWiki; AP2S1; -.
DR GenomeRNAi; 1175; -.
DR Pharos; P53680; Tbio.
DR PRO; PR:P53680; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P53680; protein.
DR Bgee; ENSG00000042753; Expressed in lower esophagus mucosa and 214 other tissues.
DR ExpressionAtlas; P53680; baseline and differential.
DR Genevisible; P53680; HS.
DR GO; GO:0030122; C:AP-2 adaptor complex; TAS:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; TAS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; TAS:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IC:ComplexPortal.
DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd14833; AP2_sigma; 1.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR027156; APS2.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11753; PTHR11753; 1.
DR PANTHER; PTHR11753:SF6; PTHR11753:SF6; 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; Cell membrane; Coated pit;
KW Disease variant; Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..142
FT /note="AP-2 complex subunit sigma"
FT /id="PRO_0000193804"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 52..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9767099"
FT /id="VSP_017352"
FT VARIANT 15
FT /note="R -> C (in HHC3; there is a rightward shift in
FT Ca(2+)concentration-response curves with the mutant
FT compared to wild-type, indicating a decrease in the
FT sensitivity of cells expressing CASR to extracellular
FT calcium; dbSNP:rs397514498)"
FT /evidence="ECO:0000269|PubMed:23222959,
FT ECO:0000269|PubMed:24081735"
FT /id="VAR_069570"
FT VARIANT 15
FT /note="R -> H (in HHC3; there is a rightward shift in
FT Ca(2+)concentration-response curves with the mutant
FT compared to wild-type, indicating a decrease in the
FT sensitivity of cells expressing CASR to extracellular
FT calcium; dbSNP:rs397514499)"
FT /evidence="ECO:0000269|PubMed:23222959"
FT /id="VAR_069571"
FT VARIANT 15
FT /note="R -> L (in HHC3; there is a rightward shift in
FT Ca(2+)concentration-response curves with the mutant
FT compared to wild-type, indicating a decrease in the
FT sensitivity of cells expressing CASR to extracellular
FT calcium; dbSNP:rs397514499)"
FT /evidence="ECO:0000269|PubMed:23222959,
FT ECO:0000269|PubMed:24081735"
FT /id="VAR_069572"
FT CONFLICT 77
FT /note="N -> K (in Ref. 1; CAA65782 and 2; CAA09018)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> G (in Ref. 1; CAA65782 and 2; CAA09018)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:6URI"
SQ SEQUENCE 142 AA; 17018 MW; CA3FD868C65AEDF6 CRC64;
MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV EFRNFKIIYR
RYAGLYFCIC VDVNDNNLAY LEAIHNFVEV LNEYFHNVCE LDLVFNFYKV YTVVDEMFLA
GEIRETSQTK VLKQLLMLQS LE
