F4JP36 (HAP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein HAPLESS 2

Alternative name(s):
GENERATIVE CELL SPECIFIC 1

Gene names

Name:	HAP2
Synonyms:	GCS1
Ordered Locus Names:	At4g11720
ORF Names:	T5C23

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in male fertility. Essential for pollen tube guidance, successful gamete attachment and fertilization. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein. Cell membrane; Single-pass membrane protein. Note: Predominantly localized in a perinuclear ring. Redistribution to the cell membrane is mediated by EC1 peptides after their secretion upon sperm arrival. Ref.1 Ref.2 Ref.8
Tissue specificity	Expressed only in mature pollen, in the two sperm cells. Ref.1 Ref.2
Developmental stage	Expressed during pollen development and tube growth. Ref.2
Domain	The N-terminus domain (62-541)and the C-terminus domain (583-705) are both required for functional gamete fusion. A positive charge, and not a conserved primary amino acid sequence, is required for a functional C-terminus domain. The N-terminus domain may be involved in interactions with another membrane-bound protein on female gametes, while positively charged C-terminus may function through electrostatic interactions with the sperm plasma membrane. Ref.6 Ref.7
Disruption phenotype	Defective in pollen tube guidance. Prevents gamete interaction and fertilization, resulting in male sterility. Ref.1 Ref.2
Sequence similarities	Belongs to the HAP2 family.
Sequence caution	The sequence CAB39943.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78215.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fertilization
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Signal Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pollen sperm cell differentiation Inferred from expression pattern PubMed 21285328. Source: TAIR single fertilization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.1. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 705	681	Protein HAPLESS 2		PRO_0000416780
Regions
	Topological domain	25 – 561	537	Extracellular Potential
	Transmembrane	562 – 582	21	Helical; Potential
	Topological domain	583 – 705	123	Cytoplasmic Potential
	Compositional bias	598 – 671	74	His-rich
Experimental info
	Sequence conflict	127	1	H → P in AAY51999. Ref.1
	Sequence conflict	127	1	H → P in AAY51998. Ref.1
	Sequence conflict	127	1	H → P in BAE71143. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	F4JP36 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: 0D4BEF577DDE6786	FASTA	705	80,505
	10 20 30 40 50 60 MVNAILMACI LAGIFVGMFN EVDGIQILSK SKLEKCEKTS DSGNLNCSTK IVLNLAVPSG 70 80 90 100 110 120 SSGGEASIVA EIVEVEDNSS SNMQTVRIPP VITVNKSAAY ALYDLTYIRD VPYKPQEYHV 130 140 150 160 170 180 TTRKCEHDAG PDIVQICERL RDEKGNVLEQ TQPICCPCGP QRRMPSSCGD IFDKMIKGKA 190 200 210 220 230 240 NTAHCLRFPG DWFHVFGIGQ RSLGFSVRVE LKTGTRVSEV IIGPENRTAT ANDNFLKVNL 250 260 270 280 290 300 IGDFGGYTSI PSFEDFYLVI PREAAEAGQP GSLGANYSMW MLLERVRFTL DGLECNKIGV 310 320 330 340 350 360 GYEAFNTQPN FCSSPYWSCL HNQLWNFRES DINRIDRHQL PLYGLEGRFE RINQHPNAGP 370 380 390 400 410 420 HSFSIGVTET LNTNLMIELR ADDIEYVFQR SPGKIINIAI PTFEALTQFG VAAVIIKNTG 430 440 450 460 470 480 EVEASYSLTF DCSKGVAFVE EQFFIIKPKA VTTRSFKLYP TKDQAAKYIC TAILKDSQFS 490 500 510 520 530 540 EVDRAECQFS TTATVLDNGT QVTNPFQIPE TQPKGFFDSI RILWTKIING LVDFITGDTC 550 560 570 580 590 600 RNKCSSFFDF SCHIQYVCLS WMVMFGLLLA LFPITCLLLW LLHQKGLFDP CYDWWEDHFD 610 620 630 640 650 660 LDHHRRLLPS RADVVNRHHH HHKHRHHHNH HRRTHQRHKH HHGQDDDVLQ KMMLERDHSD 670 680 690 700 SHYYHQLHRV HKDSKQKQRR RAKHGIVLPR DVHVERQRKQ RLRES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization." von Besser K., Frank A.C., Johnson M.A., Preuss D. Development 133:4761-4769(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: cv. Columbia. Tissue: Pollen.
[2]	"GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization." Mori T., Kuroiwa H., Higashiyama T., Kuroiwa T. Nat. Cell Biol. 8:64-71(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: cv. Columbia. Tissue: Flower.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Arabidopsis hapless mutations define essential gametophytic functions." Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D., Levin J.Z., Preuss D. Genetics 168:971-982(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[6]	"HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-terminal domain." Wong J.L., Leydon A.R., Johnson M.A. PLoS Genet. 6:E1000882-E1000882(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN.
[7]	"The functional domain of GCS1-based gamete fusion resides in the amino terminus in plant and parasite species." Mori T., Hirai M., Kuroiwa T., Miyagishima S.Y. PLoS ONE 5:E15957-E15957(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN.
[8]	"Egg cell-secreted EC1 triggers sperm cell activation during double fertilization." Sprunck S., Rademacher S., Vogler F., Gheyselinck J., Grossniklaus U., Dresselhaus T. Science 338:1093-1097(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Web resources

Protein Spotlight

A wretched tale - Issue 146 of January 2013

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ022375 mRNA. Translation: AAY51999.1. DQ022676 Genomic DNA. Translation: AAY51998.1. AB206811 mRNA. Translation: BAE71143.2. AL049500 Genomic DNA. Translation: CAB39943.1. Sequence problems. AL161532 Genomic DNA. Translation: CAB78215.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE83041.1.
IPI	IPI00545577. IPI00852274.
PIR	T04219.
RefSeq	NP_192909.2. NM_117241.2.
UniGene	At.54282.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G11720.1-P.
Proteomic databases
PRIDE	F4JP36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G11720.1; AT4G11720.1; AT4G11720.
GeneID	826777.
KEGG	ath:AT4G11720.
Organism-specific databases
TAIR	At4g11720.
Phylogenomic databases
eggNOG	NOG77705.
HOGENOM	HOG000084108.
InParanoid	Q1AP31.
OMA	HVFGIGQ.
Gene expression databases
ArrayExpress	F4JP36.
Family and domain databases
InterPro	IPR018928. Generative_cell_HAP2/GCS1. [Graphical view]
Pfam	PF10699. HAP2-GCS1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HAP2_ARATH

Accession

Primary (citable) accession number: F4JP36
Secondary accession number(s): Q1AP31, Q2PGG6, Q9T0D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program