HAP2_CHLRE
ID HAP2_CHLRE Reviewed; 1139 AA.
AC A4GRC6; Q2PGG4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Hapless 2;
DE Short=HAP2 {ECO:0000303|PubMed:18367645};
DE AltName: Full=Generative cell specific-1 {ECO:0000303|PubMed:16378100};
DE Flags: Precursor;
GN Name=HAP2 {ECO:0000303|PubMed:18367645, ECO:0000303|PubMed:25655701,
GN ECO:0000312|EMBL:ABO29824.2}; Synonyms=GCS1 {ECO:0000303|PubMed:25655701};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000312|EMBL:ABO29824.2};
RN [1] {ECO:0000312|EMBL:ABO29824.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=6145C {ECO:0000312|EMBL:ABO29824.2};
RX PubMed=18367645; DOI=10.1101/gad.1656508;
RA Liu Y., Tewari R., Ning J., Blagborough A.M., Garbom S., Pei J.,
RA Grishin N.V., Steele R.E., Sinden R.E., Snell W.J., Billker O.;
RT "The conserved plant sterility gene HAP2 functions after attachment of
RT fusogenic membranes in Chlamydomonas and Plasmodium gametes.";
RL Genes Dev. 22:1051-1068(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3] {ECO:0000312|EMBL:BAE71145.2}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-747, AND DEVELOPMENTAL STAGE.
RX PubMed=16378100; DOI=10.1038/ncb1345;
RA Mori T., Kuroiwa H., Higashiyama T., Kuroiwa T.;
RT "GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization.";
RL Nat. Cell Biol. 8:64-71(2006).
RN [4] {ECO:0000312|EMBL:ABO29824.2}
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND PROTEOLYTIC DEGRADATION.
RC STRAIN=6145C {ECO:0000312|EMBL:ABO29824.2};
RX PubMed=20335357; DOI=10.1242/dev.044743;
RA Liu Y., Misamore M.J., Snell W.J.;
RT "Membrane fusion triggers rapid degradation of two gamete-specific, fusion-
RT essential proteins in a membrane block to polygamy in Chlamydomonas.";
RL Development 137:1473-1481(2010).
RN [5]
RP REVIEW.
RX PubMed=20080406; DOI=10.1016/j.tcb.2009.12.007;
RA Wong J.L., Johnson M.A.;
RT "Is HAP2-GCS1 an ancestral gamete fusogen?";
RL Trends Cell Biol. 20:134-141(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF CYS-366; ASP-367; LYS-368; GLY-372; LEU-391; GLN-394;
RP CYS-661; 661-CYS-CYS-662 AND CYS-662.
RX PubMed=25655701; DOI=10.1242/dev.118844;
RA Liu Y., Pei J., Grishin N., Snell W.J.;
RT "The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets
RT the protein to the fusion site in Chlamydomonas and regulates the fusion
RT reaction.";
RL Development 142:962-971(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 23-592, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, DEVELOPMENTAL STAGE, MUTAGENESIS OF
RP 184-THR--ALA-186; ARG-185 AND 192-PHE-TRP-193, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-497 AND THR-577.
RX PubMed=28235200; DOI=10.1016/j.cell.2017.01.024;
RA Fedry J., Liu Y., Pehau-Arnaudet G., Pei J., Li W., Tortorici M.A.,
RA Traincard F., Meola A., Bricogne G., Grishin N.V., Snell W.J., Rey F.A.,
RA Krey T.;
RT "The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein.";
RL Cell 168:904-915(2017).
CC -!- FUNCTION: During fertilization, required on male (minus) gametes for
CC their fusion with female (plus) gametes (PubMed:18367645,
CC PubMed:20335357, PubMed:25655701, PubMed:28235200). Required for
CC membrane fusion, but not for the initial adhesion between gametes
CC (PubMed:18367645, PubMed:25655701, PubMed:28235200). Inserts (via its
CC extracellular domain) into lipid membranes (in vitro)
CC (PubMed:28235200). Probably initiates the fusion of gamete cell
CC membranes by inserting its extracellular domain into the cell membrane
CC of a female gamete (PubMed:28235200). {ECO:0000269|PubMed:18367645,
CC ECO:0000269|PubMed:20335357, ECO:0000269|PubMed:25655701,
CC ECO:0000269|PubMed:28235200}.
CC -!- SUBUNIT: Monomer. Homotrimer. Membrane contact and insertion (via its
CC extracellular domain) into a lipid membrane probably triggers
CC trimerization. {ECO:0000269|PubMed:28235200}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20335357,
CC ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:28235200,
CC ECO:0000305|PubMed:20335357, ECO:0000305|PubMed:25655701}. Cell
CC projection {ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25655701}. Note=In
CC male gametes, detected both in cytoplasmic vesicles and on cell
CC projections called mating structures at the cell membrane.
CC {ECO:0000269|PubMed:25655701}.
CC -!- DEVELOPMENTAL STAGE: Detected on male (minus) gametes (at protein
CC level) (PubMed:20335357, PubMed:25655701, PubMed:28235200). Detected at
CC low levels in vegetative cells. Highly expressed in male (minus)
CC gametes, with low expression in female (plus) gametes
CC (PubMed:16378100). {ECO:0000269|PubMed:16378100,
CC ECO:0000269|PubMed:20335357, ECO:0000269|PubMed:25655701,
CC ECO:0000269|PubMed:28235200}.
CC -!- DOMAIN: Both the cytoplasmic and the extracellular domain are required
CC for normal trafficking to the cell surface, and thus for fertilization
CC (PubMed:25655701). The extracellular domain can insert itself into
CC lipid membranes, probably as a trimer (PubMed:28235200). The
CC extracellular domain has structural similarity to class II viral fusion
CC proteins. {ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}.
CC -!- PTM: The protein present at the cell membrane is rapidly degraded after
CC fusion between male (minus) and female (plus) gametes, contrary to the
CC protein present in intracellular pools (PubMed:20335357). This may
CC represent a mechanism to avoid fusion of several male gametes with a
CC single female gamete (Probable). {ECO:0000269|PubMed:20335357,
CC ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20335357}.
CC -!- DISRUPTION PHENOTYPE: No effect on normal adhesion of male (minus)
CC gametes and female (plus) gametes, but the gametes fail to fuse and to
CC give rise to quadriflagellated zygotes. {ECO:0000269|PubMed:18367645}.
CC -!- MISCELLANEOUS: HAP2/GCS1 family members mediate membrane fusion between
CC gametes in a broad range of eukaryotes, ranging from algae and higher
CC plants to protozoans and cnidaria, suggesting they are derived from an
CC ancestral gamete fusogen (PubMed:20080406). They function similar to
CC viral fusogens, by inserting part of their extracellular domain into
CC the lipid bilayer of an adjoining cell (PubMed:28235200).
CC {ECO:0000269|PubMed:28235200, ECO:0000303|PubMed:20080406}.
CC -!- SIMILARITY: Belongs to the HAP2/GCS1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Becoming one - Issue 193 of
CC July 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/193/";
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DR EMBL; EF397563; ABO29824.2; -; mRNA.
DR EMBL; DS496135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB206813; BAE71145.2; -; mRNA.
DR PDB; 5MF1; X-ray; 3.30 A; A/B/C=23-592.
DR PDB; 6DBS; X-ray; 2.60 A; A/B/C=23-582.
DR PDB; 6E18; X-ray; 2.60 A; A=23-591.
DR PDBsum; 5MF1; -.
DR PDBsum; 6DBS; -.
DR PDBsum; 6E18; -.
DR AlphaFoldDB; A4GRC6; -.
DR SMR; A4GRC6; -.
DR STRING; 3055.EDP01230; -.
DR TCDB; 1.N.3.1.6; the hapless2 male gamete fusion factor (fusexin) family.
DR iPTMnet; A4GRC6; -.
DR eggNOG; ENOG502QREH; Eukaryota.
DR GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; IDA:UniProtKB.
DR InterPro; IPR040326; HAP2/GCS1.
DR InterPro; IPR018928; HAP2/GCS1_dom.
DR PANTHER; PTHR31764; PTHR31764; 1.
DR Pfam; PF10699; HAP2-GCS1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Fertilization; Glycoprotein; Lipid-binding; Membrane;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1139
FT /note="Hapless 2"
FT /id="PRO_5002668632"
FT TOPO_DOM 23..630
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..1139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 241..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT CARBOHYD 577
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 33..44
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 136..164
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 147..210
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 165..383
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 167..190
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 366..390
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 475..482
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT DISULFID 515..556
FT /evidence="ECO:0000269|PubMed:28235200,
FT ECO:0007744|PDB:5MF1"
FT MUTAGEN 184..186
FT /note="Missing: No effect on expression at the cell
FT surface. Abolishes ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:28235200"
FT MUTAGEN 185..186
FT /note="RA->AR: No effect on expression at the cell surface.
FT Abolishes ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:28235200"
FT MUTAGEN 185
FT /note="R->A,Q: No effect on expression at the cell surface.
FT Impairs ability to bind to lipid membranes. Abolishes
FT ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:28235200"
FT MUTAGEN 185
FT /note="R->K: No effect on expression at the cell surface.
FT No effect on binding to lipid membranes and on ability to
FT mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:28235200"
FT MUTAGEN 192..193
FT /note="FW->AA: No effect on expression at the cell surface.
FT Nearly abolishes ability to bind lipid membranes. Decreases
FT ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:28235200"
FT MUTAGEN 366
FT /note="C->A: Decreases expression at the cell surface.
FT Decreases ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 367
FT /note="D->A: No effect on expression at the cell surface.
FT No effect on ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 368
FT /note="K->A,M,R: No effect on expression at the cell
FT surface. No effect on ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 372
FT /note="G->A: No effect on expression at the cell surface.
FT No effect on ability to mediate gamete fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 391
FT /note="L->G: Abolishes expression at the cell surface.
FT Abolishes ability to mediate gamete fusion; when associated
FT with P-394."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 394
FT /note="Q->P: Abolishes expression at the cell surface.
FT Abolishes ability to mediate gamete fusion; when associated
FT with G-391."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 661..662
FT /note="CC->SS: No effect on expression at the cell surface
FT mating structure. Abolishes ability to mediate gamete
FT fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 661
FT /note="C->S: No effect on expression at the cell surface
FT mating structure. Slightly decreases ability to mediate
FT gamete fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT MUTAGEN 662
FT /note="C->S: No effect on expression at the cell surface
FT mating structure. No effect on ability to mediate gamete
FT fusion."
FT /evidence="ECO:0000269|PubMed:25655701"
FT CONFLICT 697
FT /note="L -> Q (in Ref. 3; BAE71145)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="P -> PQ (in Ref. 3; BAE71145)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="G -> V (in Ref. 3; BAE71145)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="G -> A (in Ref. 3; BAE71145)"
FT /evidence="ECO:0000305"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:6E18"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 42..54
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5MF1"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6DBS"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5MF1"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6DBS"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6DBS"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6DBS"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6E18"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:6E18"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:6E18"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6E18"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 551..561
FT /evidence="ECO:0007829|PDB:6E18"
FT STRAND 567..578
FT /evidence="ECO:0007829|PDB:6E18"
SQ SEQUENCE 1139 AA; 115204 MW; 10686ACC371BBE93 CRC64;
MCRAIAVALI VYLAQHYILA HAEVIASGRL EKCVVDGVTE ELDCQEKVVV TLTVGNGQSL
QTEALEFSLS CLNSPDGRCP CSCSAADPTC ACRDLAAPLR VSLTKSPLWA SYPLQYLSSF
NWKPLEVILR PSNKVCKDGD WEDSPTCGWF SQGGVRVADS QGFCCECSSS QVWDDTFGSS
KERTRANLDC DFWSDPLDIL IGRKPVSAHC LTFDPQWYSG YELGAASLQF EIAITVEVPT
APSPTTATTS ATPRTNNSSS ANSTNSTNSP APQFLSPPAP STREVLHLGP SVPLASSASR
LLSAKLLGDL AMYTQLPAIS NQVLMVPQPP AAAAATGSPL DATLATNRSA WMLLDKTMLS
MDGLACDKVG TGFSAFRYQP SGCGRAPQAC LSGQLKDLWE ADLARIADGR VPLYMITRFT
GGSDTTLQSF SGGPLSFALP VTSHSQSLVT LSVAADGVRL VTNRSPGKIT GAAVCRFAGT
SCGGFEAVAA RGYIYVNITN TGRLDSDYTL TVSNCSSNVR PIEARTLAVR AGSAASLDPP
MELYVEDQAA AAARTCTVSL YDSVGAVTDS LTLSFYTNAT QLVVKPSGGY NGTGDGAGVK
RNGTDCSTAC TNPIDVLCFV TKKCWSKFGR LLGIIGGALV GLGLLAVALK FGWLASLAAS
CCGGGGGAAA GGAGGGMGLG TGGGGGCFGG GQQQQQLPPA ASHAMSPPQQ QQRSHAEVAA
GAAVAGAGAA GAAAAVLGAK HGGGGGGARG KQQHADTRHL QDRDSRAIDG GASIGSSSAG
GSSSLSSYSQ PREAGGRLLQ PPAAAVFVPE GGGGGAAGDE GARAQSSDWD ARGRSPRVAD
EHGSPRQRYD GVRQSPYMVS ANPYDGWYDG GSGGGGGGGG GGYGREAPPP QGPPPHPVGA
PPPPPRRRSL WERMWLQRPG GGGGGGGGGG GGGGGGSGGG VDQHGGRSCA DAARRGGGGP
GGMRGVEGLM SNGGRPNGPH PHAPPPPPPP QQQQQQQRQR RSFLESLTAM MTLPWGGGRE
EEAGGDRRGG GRGGAAAAHG GRGAGGGRGH PPSIGSPPPG PLQPPEYGPQ GGQARRWGAG
GGRGGVGGDG GGGGVGAAAY VQLSTGGRGG GGGGGRGRGG GREGPTWHNP VYDWQAPPK
