HAP2B_ORYSJ
ID HAP2B_ORYSJ Reviewed; 714 AA.
AC B9G4M9; Q651M1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Protein HAPLESS 2-B;
DE Flags: Precursor;
GN Name=HAP2B; OrderedLocusNames=Os09g0525700, LOC_Os09g35720;
GN ORFNames=OJ1439_F07.5, OsJ_30063, OSJNBa0047P18.33;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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).
CC -!- FUNCTION: Required for male fertility. Plays a role in pollen tube
CC guidance and successful gamete attachment. Essential for the fusion of
CC gametes during double fertilization, where one male gamete fuses with
CC the egg to produce a zygote, and another male gamete fuses with the
CC central cell to produce the endosperm. Mediates the fusion of cell
CC membranes. Not required for pollen tube outgrowth.
CC {ECO:0000250|UniProtKB:F4JP36}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F4JP36}; Single-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:F4JP36}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:F4JP36}.
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. They function similar to viral fusogens, by
CC inserting part of their extracellular domain into the lipid bilayer of
CC an adjoining cell. {ECO:0000303|PubMed:20080406}.
CC -!- SIMILARITY: Belongs to the HAP2/GCS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD46352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD46496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF25636.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP005681; BAD46352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005864; BAD46496.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF25636.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000146; EEE70077.1; -; Genomic_DNA.
DR AlphaFoldDB; B9G4M9; -.
DR SMR; B9G4M9; -.
DR STRING; 4530.OS09T0525700-01; -.
DR PRIDE; B9G4M9; -.
DR eggNOG; ENOG502QREH; Eukaryota.
DR HOGENOM; CLU_022353_0_0_1; -.
DR InParanoid; B9G4M9; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; B9G4M9; OS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR InterPro; IPR040326; HAP2/GCS1.
DR InterPro; IPR018928; HAP2/GCS1_dom.
DR PANTHER; PTHR31764; PTHR31764; 1.
DR Pfam; PF10699; HAP2-GCS1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Fertilization;
KW Lipid-binding; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..714
FT /note="Protein HAPLESS 2-B"
FT /id="PRO_0000416782"
FT TOPO_DOM 34..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 597..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..619
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 45..59
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 134..164
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 146..194
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 165..321
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 167..177
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 304..328
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
FT DISULFID 441..479
FT /evidence="ECO:0000250|UniProtKB:A4GRC6"
SQ SEQUENCE 714 AA; 79763 MW; AB815B2AACBC0858 CRC64;
MAPRRRRRAA RSSRPLLLAL LAAAVNNFAP AGGVEVLAKS RLESCARGGS DDGRDRLTCD
SKIVVDLAVP SGSASLVARV AEVEENGTEA GEMPIRDPLI ITINKSEVYA LYDLTYLRDV
AYKPEEKFVK TRKCEPEAGA NVVKSCERLR DEKGSIIEHT EPVCCPCGPH RRVPSSCGNI
LDKVAKGKAN TAHCLRFPDD WFHVFDIGRR SLWFSIRVQV KKGSSESEVI VGPENRTVVS
EDSSLRVNLV GDFAGYTSLP SLENFYLVTP RKGVGGGQLE VLGDDFSRWM LLERVLFTLD
GLECNKIGVG YEAFRSQPNF CSSPLDSCLG DQLSKFWEID KNRVNNSQPP QYVVLGKFER
INQYPNAGVH TFSVGIPEVL NTNLMIELSA DDIEYVYQRS SGKIISINIS SFEALSQVGS
ARVKTKNIGR LEASYSLTFD CLSGINPVEE QYFIMKPDEK LIRTFDLRSS TDQASNYTCQ
AILKASDFSE LDRKESQFST TATVLNNGTQ IGSSENHTKG GIWGFFEAIK AWCAKMWHML
INFFTGTTCS TRCWSFLKFV IHGLLLVAVL WLLHRKGLFD PLYYWWDGVV GSEAQERARR
RHKRAHSHRH SHHHDAHKRH KTELAGHRRH HVLHIHDDDD PVAAAAAAEH VILRRHGRHE
AALGVQHRDG LKLNKHRRHG GKAVALLPPG EIIVRDGGGC GGVEHGDRRH HAWH
