IZUM1_HUMAN
ID IZUM1_HUMAN Reviewed; 350 AA.
AC Q8IYV9; Q6Q8P6; Q6Q8P7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Izumo sperm-egg fusion protein 1 {ECO:0000305};
DE AltName: Full=Oocyte binding/fusion factor {ECO:0000303|PubMed:15759005};
DE Short=OBF {ECO:0000303|PubMed:15759005};
DE AltName: Full=Sperm-specific protein izumo {ECO:0000303|PubMed:15759005};
DE Flags: Precursor;
GN Name=IZUMO1 {ECO:0000303|PubMed:15759005, ECO:0000312|HGNC:HGNC:28539};
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, TISSUE SPECIFICITY, AND
RP VARIANT VAL-333.
RC TISSUE=Testis;
RX PubMed=15759005; DOI=10.1038/nature03362;
RA Inoue N., Ikawa M., Isotani A., Okabe M.;
RT "The immunoglobulin superfamily protein Izumo is required for sperm to fuse
RT with eggs.";
RL Nature 434:234-238(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RA Li H., Zhou G., Shen C., Ke R., Zhong G., Lin L., Yang S.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-333.
RC TISSUE=Brain;
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 X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-268 IN COMPLEX WITH IZUMO1R,
RP INTERACTION WITH IZUMO1R, SUBUNIT, DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS
RP OF GLU-71; TRP-148; HIS-157 AND ARG-160.
RX PubMed=27309818; DOI=10.1038/nature18595;
RA Aydin H., Sultana A., Li S., Thavalingam A., Lee J.E.;
RT "Molecular architecture of the human sperm IZUMO1 and egg JUNO
RT fertilization complex.";
RL Nature 534:562-565(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 22-255 IN COMPLEX WITH IZUMO1R,
RP INTERACTION WITH IZUMO1R, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF
RP TRP-148.
RX PubMed=27309808; DOI=10.1038/nature18596;
RA Ohto U., Ishida H., Krayukhina E., Uchiyama S., Inoue N., Shimizu T.;
RT "Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian
RT fertilization.";
RL Nature 534:566-569(2016).
RN [7]
RP VARIANT VAL-333.
RX PubMed=18082733; DOI=10.1016/j.fertnstert.2007.09.008;
RA Granados-Gonzalez V., Aknin-Seifer I., Touraine R.-L., Chouteau J.,
RA Wolf J.-P., Levy R.;
RT "Preliminary study on the role of the human IZUMO gene in oocyte-
RT spermatozoa fusion failure.";
RL Fertil. Steril. 90:1246-1248(2008).
CC -!- FUNCTION: Essential sperm cell-surface protein required for
CC fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg
CC (PubMed:15759005). The IZUMO1:IZUMO1R/JUNO interaction is a necessary
CC adhesion event between sperm and egg that is required for fertilization
CC but is not sufficient for cell fusion (PubMed:15759005). The ligand-
CC receptor interaction probably does not act as a membrane 'fusogen'
CC (PubMed:15759005). {ECO:0000269|PubMed:15759005}.
CC -!- SUBUNIT: Monomer (PubMed:27309808, PubMed:27309818). Monomer, homodimer
CC and homooligomer; depending on the context (By similarity). Interacts
CC with IZUMO1R/JUNO. IZUMO1 and IZUMO1R/JUNO form a complex with 1:1
CC stoichiometry (PubMed:27309808, PubMed:27309818). In gamete
CC recognition, IZUMO1R/JUNO first binds to monomeric IZUMO1 (By
CC similarity). The weak, but specific interaction with IZUMO1R/JUNO
CC induces IZUMO1 homodimerization (By similarity). The process follows a
CC tight binding phase where IZUMO1 bends the entire structure towards the
CC sperm membrane side through a thiol-disulfide exchange reaction (By
CC similarity). The molecule no longer binds to IZUMO1R/JUNO and instead
CC binds to a putative second oocyte receptor (By similarity). Interacts
CC with ACE3 (By similarity). {ECO:0000250|UniProtKB:Q9D9J7,
CC ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:27309818}.
CC -!- INTERACTION:
CC Q8IYV9-1; Q8IYV9-1: IZUMO1; NbExp=2; IntAct=EBI-16208297, EBI-16208297;
CC Q8IYV9-1; A6ND01-1: IZUMO1R; NbExp=13; IntAct=EBI-16208297, EBI-16208304;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15759005};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:Q9D9J7};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Localizes
CC initially to the acrosome membrane of the sperm head (both outer and
CC inner acrosomal membranes) (By similarity). During the acrosome
CC reaction, translocates to the plasma membrane (PubMed:15759005).
CC {ECO:0000250|UniProtKB:Q9D9J7, ECO:0000269|PubMed:15759005}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IYV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYV9-2; Sequence=VSP_016962, VSP_016963;
CC Name=3;
CC IsoId=Q8IYV9-3; Sequence=VSP_016960, VSP_016961;
CC -!- TISSUE SPECIFICITY: Sperm-specific (at protein level)
CC (PubMed:15759005). Detectable on sperm surface only after the acrosome
CC reaction (PubMed:15759005). {ECO:0000269|PubMed:15759005}.
CC -!- DOMAIN: The extracellular domain assumes a distinct boomerang shape
CC when not bound to IZUMO1R/JUNO (PubMed:27309818). Interaction with
CC IZUMO1R/JUNO triggers a conformation change, so that the IZUMO1
CC extracellular domain assumes an upright conformation (PubMed:27309818).
CC {ECO:0000269|PubMed:27309818}.
CC -!- DOMAIN: The cytoplasmic C-terminus region is not essential for
CC fertilization. It is however required for protein stability.
CC {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- PTM: N-glycosylated. Glycosylation is not essential for fusion and for
CC proper protein trafficking in sperm. {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- PTM: Phosphorylated. The cytoplasmic C-terminus is phosphorylated and
CC undergoes phosphorylation changes during epididymal transit.
CC {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- MISCELLANEOUS: Izumo is the name of a Japanese shrine to marriage.
CC {ECO:0000305|PubMed:15759005}.
CC -!- SIMILARITY: Belongs to the Izumo family. {ECO:0000305}.
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DR EMBL; AB195682; BAD91012.1; -; mRNA.
DR EMBL; AY552609; AAS59145.1; -; mRNA.
DR EMBL; AY552610; AAS59146.1; -; mRNA.
DR EMBL; AC009002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034769; AAH34769.1; -; mRNA.
DR CCDS; CCDS12732.1; -. [Q8IYV9-1]
DR RefSeq; NP_001308794.1; NM_001321865.1.
DR RefSeq; NP_872381.2; NM_182575.2. [Q8IYV9-1]
DR RefSeq; XP_011525114.1; XM_011526812.2.
DR RefSeq; XP_011525115.1; XM_011526813.2.
DR PDB; 5F4E; X-ray; 2.40 A; A=22-254.
DR PDB; 5F4T; X-ray; 3.08 A; A=22-254.
DR PDB; 5F4V; X-ray; 2.90 A; A=22-268.
DR PDB; 5JK9; X-ray; 2.10 A; A/B/C/D/E/F=22-255.
DR PDB; 5JKC; X-ray; 2.90 A; A=22-255.
DR PDB; 5JKD; X-ray; 2.90 A; A=22-255.
DR PDB; 5JKE; X-ray; 2.86 A; A/C=22-255.
DR PDBsum; 5F4E; -.
DR PDBsum; 5F4T; -.
DR PDBsum; 5F4V; -.
DR PDBsum; 5JK9; -.
DR PDBsum; 5JKC; -.
DR PDBsum; 5JKD; -.
DR PDBsum; 5JKE; -.
DR AlphaFoldDB; Q8IYV9; -.
DR SMR; Q8IYV9; -.
DR BioGRID; 129843; 28.
DR CORUM; Q8IYV9; -.
DR DIP; DIP-62033N; -.
DR IntAct; Q8IYV9; 21.
DR STRING; 9606.ENSP00000327786; -.
DR TCDB; 8.A.55.1.1; the izumo sperm-egg fusion protein 1 (izumo1) family.
DR GlyGen; Q8IYV9; 1 site.
DR iPTMnet; Q8IYV9; -.
DR PhosphoSitePlus; Q8IYV9; -.
DR BioMuta; IZUMO1; -.
DR DMDM; 296434545; -.
DR MassIVE; Q8IYV9; -.
DR PaxDb; Q8IYV9; -.
DR PeptideAtlas; Q8IYV9; -.
DR PRIDE; Q8IYV9; -.
DR ProteomicsDB; 71246; -. [Q8IYV9-1]
DR ProteomicsDB; 71247; -. [Q8IYV9-2]
DR ABCD; Q8IYV9; 9 sequenced antibodies.
DR Antibodypedia; 31796; 134 antibodies from 22 providers.
DR DNASU; 284359; -.
DR Ensembl; ENST00000332955.7; ENSP00000327786.2; ENSG00000182264.9. [Q8IYV9-1]
DR Ensembl; ENST00000595517.5; ENSP00000471815.1; ENSG00000182264.9. [Q8IYV9-3]
DR Ensembl; ENST00000595937.5; ENSP00000470144.1; ENSG00000182264.9. [Q8IYV9-2]
DR GeneID; 284359; -.
DR KEGG; hsa:284359; -.
DR MANE-Select; ENST00000332955.7; ENSP00000327786.2; NM_182575.3; NP_872381.2.
DR UCSC; uc002pkj.3; human. [Q8IYV9-1]
DR CTD; 284359; -.
DR DisGeNET; 284359; -.
DR GeneCards; IZUMO1; -.
DR HGNC; HGNC:28539; IZUMO1.
DR HPA; ENSG00000182264; Tissue enriched (testis).
DR MIM; 609278; gene.
DR neXtProt; NX_Q8IYV9; -.
DR OpenTargets; ENSG00000182264; -.
DR PharmGKB; PA142671647; -.
DR VEuPathDB; HostDB:ENSG00000182264; -.
DR eggNOG; ENOG502SFD8; Eukaryota.
DR GeneTree; ENSGT00390000015014; -.
DR HOGENOM; CLU_044481_0_0_1; -.
DR InParanoid; Q8IYV9; -.
DR OMA; PATIINF; -.
DR OrthoDB; 813463at2759; -.
DR PhylomeDB; Q8IYV9; -.
DR TreeFam; TF338356; -.
DR PathwayCommons; Q8IYV9; -.
DR Reactome; R-HSA-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR SignaLink; Q8IYV9; -.
DR BioGRID-ORCS; 284359; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; IZUMO1; human.
DR GenomeRNAi; 284359; -.
DR Pharos; Q8IYV9; Tbio.
DR PRO; PR:Q8IYV9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IYV9; protein.
DR Bgee; ENSG00000182264; Expressed in right testis and 84 other tissues.
DR ExpressionAtlas; Q8IYV9; baseline and differential.
DR Genevisible; Q8IYV9; HS.
DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IC:HGNC-UCL.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IDA:HGNC-UCL.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR GO; GO:0035036; P:sperm-egg recognition; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029389; IZUMO.
DR InterPro; IPR032699; Izumo-Ig.
DR InterPro; IPR032700; IZUMO1.
DR PANTHER; PTHR35540; PTHR35540; 1.
DR Pfam; PF15005; IZUMO; 1.
DR Pfam; PF16706; Izumo-Ig; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW Disulfide bond; Fertilization; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..350
FT /note="Izumo sperm-egg fusion protein 1"
FT /id="PRO_0000045482"
FT TOPO_DOM 22..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 167..251
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 148..160
FT /note="Important for interaction with IZUMO1R"
FT /evidence="ECO:0000269|PubMed:27309818"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY06"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..149
FT /evidence="ECO:0000269|PubMed:27309808,
FT ECO:0000269|PubMed:27309818, ECO:0007744|PDB:5F4E,
FT ECO:0007744|PDB:5F4T, ECO:0007744|PDB:5F4V,
FT ECO:0007744|PDB:5JK9, ECO:0007744|PDB:5JKC,
FT ECO:0007744|PDB:5JKD, ECO:0007744|PDB:5JKE"
FT DISULFID 25..152
FT /evidence="ECO:0000269|PubMed:27309808,
FT ECO:0000269|PubMed:27309818, ECO:0007744|PDB:5F4E,
FT ECO:0007744|PDB:5F4T, ECO:0007744|PDB:5F4V,
FT ECO:0007744|PDB:5JK9, ECO:0007744|PDB:5JKC,
FT ECO:0007744|PDB:5JKD, ECO:0007744|PDB:5JKE"
FT DISULFID 135..159
FT /evidence="ECO:0000269|PubMed:27309808,
FT ECO:0000269|PubMed:27309818, ECO:0007744|PDB:5F4E,
FT ECO:0007744|PDB:5F4T, ECO:0007744|PDB:5F4V,
FT ECO:0007744|PDB:5JK9, ECO:0007744|PDB:5JKC,
FT ECO:0007744|PDB:5JKD, ECO:0007744|PDB:5JKE"
FT DISULFID 139..165
FT /evidence="ECO:0000269|PubMed:27309808,
FT ECO:0000269|PubMed:27309818, ECO:0007744|PDB:5F4E,
FT ECO:0007744|PDB:5F4T, ECO:0007744|PDB:5F4V,
FT ECO:0007744|PDB:5JK9, ECO:0007744|PDB:5JKC,
FT ECO:0007744|PDB:5JKD, ECO:0007744|PDB:5JKE"
FT DISULFID 182..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:27309818,
FT ECO:0007744|PDB:5F4E, ECO:0007744|PDB:5F4T,
FT ECO:0007744|PDB:5F4V, ECO:0007744|PDB:5JK9,
FT ECO:0007744|PDB:5JKC, ECO:0007744|PDB:5JKD,
FT ECO:0007744|PDB:5JKE"
FT VAR_SEQ 57..68
FT /note="VENAVKDFQELS -> MRPHCKRGPGVC (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016960"
FT VAR_SEQ 69..350
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016961"
FT VAR_SEQ 167..194
FT /note="ERNVEVPQMEDMILDCELNWHQASEGLT -> GERTGPSRRNWCRAECGSSS
FT NGRHDPGL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016962"
FT VAR_SEQ 195..350
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016963"
FT VARIANT 333
FT /note="A -> V (in dbSNP:rs2307019)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15759005, ECO:0000269|PubMed:18082733"
FT /id="VAR_055399"
FT MUTAGEN 71
FT /note="E->A,K: Mildly decreases interaction with IZUMO1R."
FT /evidence="ECO:0000269|PubMed:27309818"
FT MUTAGEN 148
FT /note="W->A: Abolishes interaction with IZUMO1R."
FT /evidence="ECO:0000269|PubMed:27309818"
FT MUTAGEN 157
FT /note="H->A: Nearly abolishes interaction with IZUMO1R."
FT /evidence="ECO:0000269|PubMed:27309818"
FT MUTAGEN 160
FT /note="R->A,E: Nearly abolishes interaction with IZUMO1R."
FT /evidence="ECO:0000269|PubMed:27309818"
FT CONFLICT 36
FT /note="L -> P (in Ref. 2; AAS59145)"
FT /evidence="ECO:0000305"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5F4E"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 104..132
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:5JK9"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5F4T"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 191..201
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5F4E"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:5JK9"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 229..241
FT /evidence="ECO:0007829|PDB:5JK9"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:5JK9"
SQ SEQUENCE 350 AA; 38930 MW; 8741BB3F93ABCFA9 CRC64;
MGPHFTLLCA ALAGCLLPAE GCVICDPSVV LALKSLEKDY LPGHLDAKHH KAMMERVENA
VKDFQELSLN EDAYMGVVDE ATLQKGSWSL LKDLKRITDS DVKGDLFVKE LFWMLHLQKE
TFATYVARFQ KEAYCPNKCG VMLQTLIWCK NCKKEVHACR KSYDCGERNV EVPQMEDMIL
DCELNWHQAS EGLTDYSFYR VWGNNTETLV SKGKEATLTK PMVGPEDAGS YRCELGSVNS
SPATIINFHV TVLPKMIKEE KPSPNIVTPG EATTESSISL QPLQPEKMLA SRLLGLLICG
SLALITGLTF AIFRRRKVID FIKSSLFGLG SGAAEQTQVP KEKATDSRQQ
