AQP4_HUMAN
ID AQP4_HUMAN Reviewed; 323 AA.
AC P55087; P78564;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Aquaporin-4;
DE Short=AQP-4;
DE AltName: Full=Mercurial-insensitive water channel {ECO:0000303|PubMed:7559426};
DE Short=MIWC {ECO:0000303|PubMed:7559426};
DE AltName: Full=WCH4;
GN Name=AQP4;
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] {ECO:0000312|EMBL:AAC50284.1, ECO:0000312|EMBL:AAC52112.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=7559426; DOI=10.1074/jbc.270.39.22907;
RA Yang B., Ma T., Verkman A.S.;
RT "cDNA cloning, gene organization, and chromosomal localization of a human
RT mercurial insensitive water channel. Evidence for distinct transcriptional
RT units.";
RL J. Biol. Chem. 270:22907-22913(1995).
RN [2] {ECO:0000312|EMBL:BAA09715.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=8601457; DOI=10.1016/0014-5793(96)00092-0;
RA Misaka T., Abe K., Iwabuchi K., Kusakabe Y., Ichinose M., Miki K.,
RA Emori Y., Arai S.;
RT "A water channel closely related to rat brain aquaporin 4 is expressed in
RT acid- and pepsinogen-secretory cells of human stomach.";
RL FEBS Lett. 381:208-212(1996).
RN [3] {ECO:0000312|EMBL:AAB26957.1, ECO:0000312|EMBL:AAB26958.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8855281; DOI=10.1073/pnas.93.20.10908;
RA Lu M., Lee M.D., Smith B.L., Jung J.S., Agre P., Verdijk M.A.J., Merkx G.,
RA Rijss J.P.L., Deen P.M.T.;
RT "The human AQP4 gene: definition of the locus encoding two water channel
RT polypeptides in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10908-10912(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 SUBUNIT.
RX PubMed=22328087; DOI=10.1093/hmg/dds032;
RA Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C.,
RA Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C., Ambrosini E.;
RT "Megalencephalic leukoencephalopathy with subcortical cysts protein 1
RT functionally cooperates with the TRPV4 cation channel to activate the
RT response of astrocytes to osmotic stress: dysregulation by pathological
RT mutations.";
RL Hum. Mol. Genet. 21:2166-2180(2012).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29055082; DOI=10.1111/jcmm.13401;
RA Rosito S., Nicchia G.P., Palazzo C., Lia A., Buccoliero C., Pisani F.,
RA Svelto M., Trojano M., Frigeri A.;
RT "Supramolecular aggregation of aquaporin-4 is different in muscle and
RT brain: correlation with tissue susceptibility in neuromyelitis optica.";
RL J. Cell. Mol. Med. 22:1236-1246(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-254, FUNCTION, TOPOLOGY,
RP SUBUNIT, AND DOMAIN.
RX PubMed=19383790; DOI=10.1073/pnas.0902725106;
RA Ho J.D., Yeh R., Sandstrom A., Chorny I., Harries W.E., Robbins R.A.,
RA Miercke L.J., Stroud R.M.;
RT "Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of
RT conductance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7437-7442(2009).
CC -!- FUNCTION: Forms a water-specific channel (PubMed:7559426,
CC PubMed:8601457, PubMed:19383790). Plays an important role in brain
CC water homeostasis and in glymphatic solute transport. Required for a
CC normal rate of water exchange across the blood brain interface.
CC Required for normal levels of cerebrospinal fluid influx into the brain
CC cortex and parenchyma along paravascular spaces that surround
CC penetrating arteries, and for normal drainage of interstitial fluid
CC along paravenous drainage pathways. Thereby, it is required for normal
CC clearance of solutes from the brain interstitial fluid, including
CC soluble beta-amyloid peptides derived from APP. Plays a redundant role
CC in urinary water homeostasis and urinary concentrating ability (By
CC similarity). {ECO:0000250|UniProtKB:P55088,
CC ECO:0000269|PubMed:19383790, ECO:0000269|PubMed:7559426,
CC ECO:0000269|PubMed:8601457}.
CC -!- SUBUNIT: Homotetramer (PubMed:19383790). The tetramers can form
CC oligomeric arrays in membranes. The size of the oligomers differs
CC between tissues and is smaller in skeletal muscle than in brain.
CC Interaction between AQP4 oligomeric arrays in close-by cells can
CC contribute to cell-cell adhesion (By similarity). Part of a complex
CC containing MLC1, TRPV4, HEPACAM and ATP1B1 (PubMed:22328087).
CC {ECO:0000250|UniProtKB:P47863, ECO:0000269|PubMed:19383790,
CC ECO:0000269|PubMed:22328087}.
CC -!- INTERACTION:
CC P55087; O43889-2: CREB3; NbExp=3; IntAct=EBI-10104898, EBI-625022;
CC P55087; P48165: GJA8; NbExp=3; IntAct=EBI-10104898, EBI-17458373;
CC P55087; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-10104898, EBI-744820;
CC P55087; Q5T9L3-1: WLS; NbExp=3; IntAct=EBI-10104898, EBI-22114623;
CC P55087-1; P55087-1: AQP4; NbExp=2; IntAct=EBI-15771758, EBI-15771758;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7559426,
CC ECO:0000269|PubMed:8601457}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19383790}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P55088}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19383790}. Endosome membrane
CC {ECO:0000250|UniProtKB:P47863}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:29055082}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19383790}. Cell projection
CC {ECO:0000250|UniProtKB:P47863}. Note=Activation of the vasopressin
CC receptor AVPR1A triggers AQP4 phosphorylation at Ser-180 and promotes
CC its internalization from the cell membrane. Detected on brain astrocyte
CC processes and astrocyte endfeet close to capillaries.
CC {ECO:0000250|UniProtKB:P47863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=AQP4-M1 {ECO:0000305};
CC IsoId=P55087-1; Sequence=Displayed;
CC Name=1; Synonyms=AQP4-M23 {ECO:0000305};
CC IsoId=P55087-2; Sequence=VSP_003232;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (PubMed:29055082).
CC Detected in stomach, along the glandular base region of the fundic
CC gland (at protein level) (PubMed:8601457). Detected in brain, lung and
CC skeletal muscle, and at much lower levels in heart and ovary
CC (PubMed:7559426, PubMed:8601457). {ECO:0000269|PubMed:29055082,
CC ECO:0000269|PubMed:7559426, ECO:0000269|PubMed:8601457}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). {ECO:0000269|PubMed:19383790}.
CC -!- PTM: Phosphorylation by PKC at Ser-180 reduces conductance by 50%.
CC Phosphorylation by PKG at Ser-111 in response to glutamate increases
CC conductance by 40% (By similarity). {ECO:0000250}.
CC -!- PTM: Isoform 2: Palmitoylated on its N-terminal region. Isoform 1: Not
CC palmitoylated. {ECO:0000250|UniProtKB:P47863}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AQP4ID684ch18q11.html";
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DR EMBL; U34846; AAC52112.1; ALT_INIT; mRNA.
DR EMBL; U34845; AAC50284.1; -; mRNA.
DR EMBL; D63412; BAA09715.1; -; mRNA.
DR EMBL; U63622; AAB26957.1; -; mRNA.
DR EMBL; U63623; AAB26958.1; -; mRNA.
DR EMBL; AC018371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022286; AAH22286.1; -; mRNA.
DR CCDS; CCDS11889.1; -. [P55087-1]
DR CCDS; CCDS58617.1; -. [P55087-2]
DR PIR; I39178; I39178.
DR RefSeq; NP_001641.1; NM_001650.5. [P55087-1]
DR RefSeq; NP_004019.1; NM_004028.4. [P55087-2]
DR PDB; 3GD8; X-ray; 1.80 A; A=32-254.
DR PDBsum; 3GD8; -.
DR AlphaFoldDB; P55087; -.
DR SMR; P55087; -.
DR BioGRID; 106857; 10.
DR CORUM; P55087; -.
DR DIP; DIP-48842N; -.
DR IntAct; P55087; 5.
DR STRING; 9606.ENSP00000372654; -.
DR ChEMBL; CHEMBL5964; -.
DR TCDB; 1.A.8.8.5; the major intrinsic protein (mip) family.
DR GlyGen; P55087; 2 sites.
DR iPTMnet; P55087; -.
DR PhosphoSitePlus; P55087; -.
DR SwissPalm; P55087; -.
DR BioMuta; AQP4; -.
DR DMDM; 2506859; -.
DR MassIVE; P55087; -.
DR PaxDb; P55087; -.
DR PeptideAtlas; P55087; -.
DR PRIDE; P55087; -.
DR ProteomicsDB; 56788; -. [P55087-1]
DR ProteomicsDB; 56789; -. [P55087-2]
DR Antibodypedia; 3103; 580 antibodies from 37 providers.
DR DNASU; 361; -.
DR Ensembl; ENST00000383168.9; ENSP00000372654.4; ENSG00000171885.18. [P55087-1]
DR Ensembl; ENST00000440832.7; ENSP00000393121.3; ENSG00000171885.18. [P55087-2]
DR Ensembl; ENST00000581374.5; ENSP00000462597.1; ENSG00000171885.18. [P55087-2]
DR Ensembl; ENST00000672188.1; ENSP00000500720.1; ENSG00000171885.18. [P55087-1]
DR GeneID; 361; -.
DR KEGG; hsa:361; -.
DR MANE-Select; ENST00000383168.9; ENSP00000372654.4; NM_001650.7; NP_001641.1.
DR UCSC; uc002kvz.4; human. [P55087-1]
DR CTD; 361; -.
DR DisGeNET; 361; -.
DR GeneCards; AQP4; -.
DR HGNC; HGNC:637; AQP4.
DR HPA; ENSG00000171885; Group enriched (brain, lung).
DR MIM; 600308; gene.
DR neXtProt; NX_P55087; -.
DR OpenTargets; ENSG00000171885; -.
DR PharmGKB; PA24922; -.
DR VEuPathDB; HostDB:ENSG00000171885; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000156037; -.
DR InParanoid; P55087; -.
DR OMA; CRREDIM; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P55087; -.
DR TreeFam; TF312940; -.
DR PathwayCommons; P55087; -.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; P55087; -.
DR SIGNOR; P55087; -.
DR BioGRID-ORCS; 361; 7 hits in 1060 CRISPR screens.
DR ChiTaRS; AQP4; human.
DR EvolutionaryTrace; P55087; -.
DR GeneWiki; Aquaporin_4; -.
DR GenomeRNAi; 361; -.
DR Pharos; P55087; Tbio.
DR PRO; PR:P55087; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P55087; protein.
DR Bgee; ENSG00000171885; Expressed in lateral globus pallidus and 153 other tissues.
DR ExpressionAtlas; P55087; baseline and differential.
DR Genevisible; P55087; HS.
DR GO; GO:0097450; C:astrocyte end-foot; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:Ensembl.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IEP:UniProtKB.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0030104; P:water homeostasis; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; IDA:UniProtKB.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Endosome; Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..323
FT /note="Aquaporin-4"
FT /id="PRO_0000063948"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 58..69
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 90..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19383790"
FT INTRAMEM 94..101
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 137..155
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 177..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 206..208
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19383790"
FT INTRAMEM 209..222
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 223..231
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19383790"
FT TOPO_DOM 253..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19383790"
FT MOTIF 97..99
FT /note="NPA 1"
FT /evidence="ECO:0000305|PubMed:19383790"
FT MOTIF 213..215
FT /note="NPA 2"
FT /evidence="ECO:0000305|PubMed:19383790"
FT MOD_RES 111
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000250|UniProtKB:P55088"
FT MOD_RES 180
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P47863"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47863"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55088"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55088"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47863"
FT LIPID 13
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P47863"
FT LIPID 17
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P47863"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_003232"
FT CONFLICT 246
FT /note="G -> A (in Ref. 1; AAC52112)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="VE -> AK (in Ref. 1; AAC52112)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="P -> L (in Ref. 1; AAC52112)"
FT /evidence="ECO:0000305"
FT HELIX 33..55
FT /evidence="ECO:0007829|PDB:3GD8"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 70..92
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 112..136
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3GD8"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 156..177
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 189..208
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:3GD8"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:3GD8"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:3GD8"
SQ SEQUENCE 323 AA; 34830 MW; 1A1600CF0DC11052 CRC64;
MSDRPTARRW GKCGPLCTRE NIMVAFKGVW TQAFWKAVTA EFLAMLIFVL LSLGSTINWG
GTEKPLPVDM VLISLCFGLS IATMVQCFGH ISGGHINPAV TVAMVCTRKI SIAKSVFYIA
AQCLGAIIGA GILYLVTPPS VVGGLGVTMV HGNLTAGHGL LVELIITFQL VFTIFASCDS
KRTDVTGSIA LAIGFSVAIG HLFAINYTGA SMNPARSFGP AVIMGNWENH WIYWVGPIIG
AVLAGGLYEY VFCPDVEFKR RFKEAFSKAA QQTKGSYMEV EDNRSQVETD DLILKPGVVH
VIDVDRGEEK KGKDQSGEVL SSV
