AQP10_HUMAN
ID AQP10_HUMAN Reviewed; 301 AA.
AC Q96PS8; Q5VYD3; Q5VYD4; Q8NG70;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Aquaporin-10;
DE Short=AQP-10;
DE AltName: Full=Aquaglyceroporin-10;
DE AltName: Full=Small intestine aquaporin;
GN Name=AQP10;
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 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Jejunum;
RX PubMed=11573934; DOI=10.1006/bbrc.2001.5661;
RA Hatakeyama S., Yoshida Y., Tani T., Koyama Y., Nihei K., Ohshiro K.,
RA Kamiie J., Yaoita E., Suda T., Hatakeyama K., Yamamoto T.;
RT "Cloning of a new aquaporin (AQP10) abundantly expressed in duodenum and
RT jejunum.";
RL Biochem. Biophys. Res. Commun. 287:814-819(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12084581; DOI=10.1016/s0167-4781(02)00393-7;
RA Ishibashi K., Morinaga T., Kuwahara M., Sasaki S., Imai M.;
RT "Cloning and identification of a new member of water channel (AQP10) as an
RT aquaglyceroporin.";
RL Biochim. Biophys. Acta 1576:335-340(2002).
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 MRNA] (ISOFORM 1).
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15221416; DOI=10.1007/s00418-004-0657-1;
RA Mobasheri A., Shakibaei M., Marples D.;
RT "Immunohistochemical localization of aquaporin 10 in the apical membranes
RT of the human ileum: a potential pathway for luminal water and small solute
RT absorption.";
RL Histochem. Cell Biol. 121:463-471(2004).
RN [6]
RP FUNCTION, GLYCOSYLATION AT ASN-133, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND MUTAGENESIS OF ASN-133.
RX PubMed=21733844; DOI=10.1074/jbc.m111.242677;
RA Oeberg F., Sjoehamn J., Fischer G., Moberg A., Pedersen A., Neutze R.,
RA Hedfalk K.;
RT "Glycosylation increases the thermostability of human aquaporin 10
RT protein.";
RL J. Biol. Chem. 286:31915-31923(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23382902; DOI=10.1371/journal.pone.0054474;
RA Laforenza U., Scaffino M.F., Gastaldi G.;
RT "Aquaporin-10 represents an alternative pathway for glycerol efflux from
RT human adipocytes.";
RL PLoS ONE 8:E54474-E54474(2013).
RN [8] {ECO:0007744|PDB:6F7H}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-27; GLY-73; SER-77; HIS-80; PHE-85
RP AND ARG-94.
RX PubMed=30420639; DOI=10.1038/s41467-018-07176-z;
RA Gotfryd K., Mosca A.F., Missel J.W., Truelsen S.F., Wang K., Spulber M.,
RA Krabbe S., Helix-Nielsen C., Laforenza U., Soveral G., Pedersen P.A.,
RA Gourdon P.;
RT "Human adipose glycerol flux is regulated by a pH gate in AQP10.";
RL Nat. Commun. 9:4749-4749(2018).
CC -!- FUNCTION: [Isoform 1]: Water channel that mediates water transport
CC across cell membranes irrespective of the cytosolic pH
CC (PubMed:12084581, PubMed:21733844, PubMed:23382902, PubMed:30420639).
CC The channel is permeable to glycerol, especially when the cytosolic pH
CC is acidified (PubMed:21733844, PubMed:30420639). Contributes to
CC adipocyte water and glycerol permeability, and may thereby contribute
CC to the utilization of glycerol derived from phospholipid degradation
CC (PubMed:23382902). May contribute to water transport in the intestine
CC (Probable). {ECO:0000269|PubMed:12084581, ECO:0000269|PubMed:21733844,
CC ECO:0000269|PubMed:23382902, ECO:0000269|PubMed:30420639,
CC ECO:0000305|PubMed:11573934, ECO:0000305|PubMed:12084581,
CC ECO:0000305|PubMed:15221416}.
CC -!- FUNCTION: [Isoform 2]: Water channel that mediates water transport
CC across cell membranes, but that is not permeable to glycerol.
CC {ECO:0000269|PubMed:11573934}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:30420639}.
CC -!- INTERACTION:
CC Q96PS8; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12820279, EBI-11343438;
CC Q96PS8; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12820279, EBI-1045797;
CC Q96PS8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12820279, EBI-6942903;
CC Q96PS8; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-12820279, EBI-2680384;
CC Q96PS8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12820279, EBI-781551;
CC Q96PS8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12820279, EBI-13345167;
CC Q96PS8; O60883: GPR37L1; NbExp=3; IntAct=EBI-12820279, EBI-2927498;
CC Q96PS8; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12820279, EBI-8632435;
CC Q96PS8; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-12820279, EBI-10329546;
CC Q96PS8; O14880: MGST3; NbExp=3; IntAct=EBI-12820279, EBI-724754;
CC Q96PS8; O14524-2: NEMP1; NbExp=3; IntAct=EBI-12820279, EBI-10969203;
CC Q96PS8; O15173: PGRMC2; NbExp=3; IntAct=EBI-12820279, EBI-1050125;
CC Q96PS8; P60201-2: PLP1; NbExp=3; IntAct=EBI-12820279, EBI-12188331;
CC Q96PS8; P15151: PVR; NbExp=3; IntAct=EBI-12820279, EBI-3919694;
CC Q96PS8; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-12820279, EBI-3920694;
CC Q96PS8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12820279, EBI-17247926;
CC Q96PS8; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12820279, EBI-17280858;
CC Q96PS8; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-12820279, EBI-8032987;
CC Q96PS8; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-12820279, EBI-17684533;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:15221416}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30420639}. Cell membrane
CC {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581,
CC ECO:0000269|PubMed:23382902, ECO:0000269|PubMed:30420639}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:30420639}. Lipid droplet
CC {ECO:0000269|PubMed:23382902}. Note=Detected around lipid droplets.
CC {ECO:0000269|PubMed:23382902}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PS8-2; Sequence=VSP_010211;
CC -!- TISSUE SPECIFICITY: Detected in epithelial cells on villi in the ileum,
CC and also in stomach, jejunum, colon, rectum, white adipose tissue and
CC placenta (at protein level) (PubMed:15221416, PubMed:23382902).
CC Expressed in duodenum and jejunum. Highest expression in absorptive
CC epithelial cells at the tips of villi in the jejunum (PubMed:11573934,
CC PubMed:12084581). Detected in subcutaneous adipose tissue
CC (PubMed:23382902). {ECO:0000269|PubMed:11573934,
CC ECO:0000269|PubMed:12084581, ECO:0000269|PubMed:15221416,
CC ECO:0000269|PubMed:23382902}.
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:30420639}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- CAUTION: Acidification of the cytosol strongly increases channel
CC permeability to glycerol (PubMed:30420639). Initial experiments showed
CC that isoform 2 is permeable to water, but not to glycerol, but these
CC results were obtained without lowering the cytosolic pH
CC (PubMed:11573934). {ECO:0000269|PubMed:11573934,
CC ECO:0000269|PubMed:30420639}.
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DR EMBL; AF159174; AAL25998.1; -; mRNA.
DR EMBL; AB066105; BAB91223.1; -; mRNA.
DR EMBL; AL354980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069607; AAH69607.1; -; mRNA.
DR EMBL; BC074896; AAH74896.1; -; mRNA.
DR EMBL; BC074897; AAH74897.1; -; mRNA.
DR CCDS; CCDS1065.1; -. [Q96PS8-1]
DR PIR; JC7772; JC7772.
DR RefSeq; NP_536354.2; NM_080429.2. [Q96PS8-1]
DR PDB; 6F7H; X-ray; 2.30 A; A/B/C/D=1-301.
DR PDBsum; 6F7H; -.
DR AlphaFoldDB; Q96PS8; -.
DR SMR; Q96PS8; -.
DR BioGRID; 124627; 20.
DR IntAct; Q96PS8; 19.
DR STRING; 9606.ENSP00000318355; -.
DR TCDB; 1.A.8.9.5; the major intrinsic protein (mip) family.
DR GlyGen; Q96PS8; 2 sites.
DR iPTMnet; Q96PS8; -.
DR BioMuta; AQP10; -.
DR DMDM; 47117905; -.
DR MassIVE; Q96PS8; -.
DR PaxDb; Q96PS8; -.
DR PeptideAtlas; Q96PS8; -.
DR PRIDE; Q96PS8; -.
DR Antibodypedia; 34151; 152 antibodies from 24 providers.
DR DNASU; 89872; -.
DR Ensembl; ENST00000324978.8; ENSP00000318355.3; ENSG00000143595.13. [Q96PS8-1]
DR Ensembl; ENST00000484864.1; ENSP00000420341.1; ENSG00000143595.13. [Q96PS8-2]
DR GeneID; 89872; -.
DR KEGG; hsa:89872; -.
DR MANE-Select; ENST00000324978.8; ENSP00000318355.3; NM_080429.3; NP_536354.2.
DR UCSC; uc001feu.3; human. [Q96PS8-1]
DR CTD; 89872; -.
DR DisGeNET; 89872; -.
DR GeneCards; AQP10; -.
DR HGNC; HGNC:16029; AQP10.
DR HPA; ENSG00000143595; Tissue enriched (intestine).
DR MIM; 606578; gene.
DR neXtProt; NX_Q96PS8; -.
DR OpenTargets; ENSG00000143595; -.
DR PharmGKB; PA24919; -.
DR VEuPathDB; HostDB:ENSG00000143595; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000162648; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; Q96PS8; -.
DR OMA; FTSHHYY; -.
DR OrthoDB; 1246320at2759; -.
DR PhylomeDB; Q96PS8; -.
DR TreeFam; TF313173; -.
DR PathwayCommons; Q96PS8; -.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; Q96PS8; -.
DR BioGRID-ORCS; 89872; 13 hits in 1072 CRISPR screens.
DR GenomeRNAi; 89872; -.
DR Pharos; Q96PS8; Tbio.
DR PRO; PR:Q96PS8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96PS8; protein.
DR Bgee; ENSG00000143595; Expressed in jejunal mucosa and 44 other tissues.
DR Genevisible; Q96PS8; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015254; F:glycerol channel activity; IDA:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA: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; IPR026252; Aquaporin_10.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02022; AQUAPORIN10M.
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; Glycoprotein;
KW Lipid droplet; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="Aquaporin-10"
FT /id="PRO_0000063967"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 47..52
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 74..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30420639"
FT INTRAMEM 78..91
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 92..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 98..122
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 123..156
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 178..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT INTRAMEM 208..226
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 227..243
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30420639"
FT TOPO_DOM 265..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30420639"
FT MOTIF 82..84
FT /note="NPA 1"
FT /evidence="ECO:0000305|PubMed:30420639"
FT MOTIF 214..216
FT /note="NPA 2"
FT /evidence="ECO:0000305|PubMed:30420639"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21733844"
FT VAR_SEQ 236..301
FT /note="SAGNGWWWVPVVAPLVGATVGTATYQLLVALHHPEGPEPAQDLVSAQHKASE
FT LETPASAQMLECKL -> RWETDSPGAGLHSPSSAKGSVPGSTALCL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11573934"
FT /id="VSP_010211"
FT VARIANT 15
FT /note="R -> Q (in dbSNP:rs6668968)"
FT /id="VAR_033519"
FT VARIANT 123
FT /note="H -> Y (in dbSNP:rs6685323)"
FT /id="VAR_050063"
FT MUTAGEN 27
FT /note="E->Q: Abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 73
FT /note="G->A: Increased permeability to glycerol at acidic
FT pH."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 73
FT /note="G->F: Abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 77
FT /note="S->A,D: Nearly abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 80
FT /note="H->A: Abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 85
FT /note="F->A: Nearly abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 94
FT /note="R->A: Abolishes permeability to glycerol."
FT /evidence="ECO:0000269|PubMed:30420639"
FT MUTAGEN 133
FT /note="N->Q: Abolishes N-glycosylation."
FT /evidence="ECO:0000269|PubMed:21733844"
FT HELIX 19..47
FT /evidence="ECO:0007829|PDB:6F7H"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 55..72
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 100..121
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:6F7H"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 156..178
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:6F7H"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:6F7H"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6F7H"
FT HELIX 244..267
FT /evidence="ECO:0007829|PDB:6F7H"
SQ SEQUENCE 301 AA; 31763 MW; CB2A7AB680548987 CRC64;
MVFTQAPAEI MGHLRIRSLL ARQCLAEFLG VFVLMLLTQG AVAQAVTSGE TKGNFFTMFL
AGSLAVTIAI YVGGNVSGAH LNPAFSLAMC IVGRLPWVKL PIYILVQLLS AFCASGATYV
LYHDALQNYT GGNLTVTGPK ETASIFATYP APYLSLNNGF LDQVLGTGML IVGLLAILDR
RNKGVPAGLE PVVVGMLILA LGLSMGANCG IPLNPARDLG PRLFTYVAGW GPEVFSAGNG
WWWVPVVAPL VGATVGTATY QLLVALHHPE GPEPAQDLVS AQHKASELET PASAQMLECK
L
