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Database: UniProt
Entry: P55087
LinkDB: P55087
Original site: P55087 
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   02-JUN-2021, entry version 184.
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   SMR; P55087; -.
DR   BioGRID; 106857; 6.
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; 567 antibodies.
DR   DNASU; 361; -.
DR   Ensembl; ENST00000383168; ENSP00000372654; ENSG00000171885. [P55087-1]
DR   Ensembl; ENST00000440832; ENSP00000393121; ENSG00000171885. [P55087-2]
DR   Ensembl; ENST00000581374; ENSP00000462597; ENSG00000171885. [P55087-2]
DR   Ensembl; ENST00000672188; ENSP00000500720; ENSG00000171885. [P55087-1]
DR   GeneID; 361; -.
DR   KEGG; hsa:361; -.
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:ENSG00000171885.13; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   GeneTree; ENSGT00940000156037; -.
DR   InParanoid; P55087; -.
DR   OMA; NWGGSEK; -.
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   SIGNOR; P55087; -.
DR   BioGRID-ORCS; 361; 2 hits in 977 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 172 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: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:0042383; C:sarcolemma; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR   GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR   GO; GO:0090660; P:cerebrospinal fluid circulation; ISS:UniProtKB.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IEP:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
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
//
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