AFF1_CAEEL
ID AFF1_CAEEL Reviewed; 589 AA.
AC G5EGL9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Cell fusion protein aff-1 {ECO:0000305|PubMed:17488621};
DE AltName: Full=Anchor cell fusion failure protein 1 {ECO:0000312|EMBL:ABP04049.1};
DE Flags: Precursor;
GN Name=aff-1 {ECO:0000312|WormBase:C44B7.3};
GN ORFNames=C44B7.3 {ECO:0000312|WormBase:C44B7.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:ABP04049.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17488621; DOI=10.1016/j.devcel.2007.03.003;
RA Sapir A., Choi J., Leikina E., Avinoam O., Valansi C., Chernomordik L.V.,
RA Newman A.P., Podbilewicz B.;
RT "AFF-1, a FOS-1-regulated fusogen, mediates fusion of the anchor cell in C.
RT elegans.";
RL Dev. Cell 12:683-698(2007).
RN [2] {ECO:0000312|EMBL:CCD61566.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD61566.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21350017; DOI=10.1242/dev.058305;
RA Procko C., Lu Y., Shaham S.;
RT "Glia delimit shape changes of sensory neuron receptive endings in C.
RT elegans.";
RL Development 138:1371-1381(2011).
CC -!- FUNCTION: Required for cell fusion events during development including
CC the fusion of anchor cells (AC), vulval A and vulval D rings, and late
CC epidermal seam cells (PubMed:17488621). Required for amphid sheath cell
CC fusion induced by entry into dauer stage (PubMed:21350017).
CC {ECO:0000269|PubMed:17488621, ECO:0000269|PubMed:21350017}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17488621};
CC Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:21350017}.
CC -!- TISSUE SPECIFICITY: Expressed in amphid sheath cells.
CC {ECO:0000269|PubMed:21350017}.
CC -!- DEVELOPMENTAL STAGE: First expressed in embryonic hyp5 cells and then
CC during larval development in pharyngeal muscles, uterine rings, head
CC and tail neurons, sheath cells of chemo-sensory neurons, and in male
CC neurons. Expressed in AC, vulval D rings and uterine seam cells in cell
CC fusion events during development. {ECO:0000269|PubMed:17488621}.
CC -!- DISRUPTION PHENOTYPE: Egg laying defective phenotype. AC fail to fuse
CC in the majority of worms (PubMed:17488621). RNAi-mediated knockdown in
CC a daf-7 e1372 mutant background causes a severe defect in amphid sheath
CC cell fusion induced by entry into dauer stage (PubMed:21350017).
CC {ECO:0000269|PubMed:17488621, ECO:0000269|PubMed:21350017}.
CC -!- SIMILARITY: Belongs to the EFF/AFF cell fusogen family. {ECO:0000305}.
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DR EMBL; EF205023; ABP04049.1; -; mRNA.
DR EMBL; FO080141; CCD61566.1; -; Genomic_DNA.
DR RefSeq; NP_495402.3; NM_063001.5.
DR AlphaFoldDB; G5EGL9; -.
DR SMR; G5EGL9; -.
DR STRING; 6239.C44B7.3; -.
DR TCDB; 1.N.4.1.4; the ff fusogen (fff) family.
DR PaxDb; G5EGL9; -.
DR EnsemblMetazoa; C44B7.3.1; C44B7.3.1; WBGene00016625.
DR GeneID; 174123; -.
DR KEGG; cel:CELE_C44B7.3; -.
DR CTD; 174123; -.
DR WormBase; C44B7.3; CE41369; WBGene00016625; aff-1.
DR eggNOG; ENOG502RRTU; Eukaryota.
DR GeneTree; ENSGT00970000196161; -.
DR HOGENOM; CLU_463248_0_0_1; -.
DR InParanoid; G5EGL9; -.
DR OMA; INEHETI; -.
DR OrthoDB; 384978at2759; -.
DR PhylomeDB; G5EGL9; -.
DR PRO; PR:G5EGL9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016625; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IMP:WormBase.
DR Gene3D; 2.60.40.3980; -; 1.
DR InterPro; IPR029213; Fusogen_EFF/AFF.
DR InterPro; IPR043076; Fusogen_EFF/AFF_dom3.
DR PANTHER; PTHR37415; PTHR37415; 1.
DR Pfam; PF14884; EFF-AFF; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..589
FT /note="Cell fusion protein aff-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432857"
FT TOPO_DOM 21..537
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 589 AA; 67463 MW; F3CB4DDFBEBFC0B4 CRC64;
MRLWQWSIAV AICLVMVTEA RLRRHHRKRR FVSSNFDEFY CGESAHAQSQ FEEERESNSS
KVSSVHSTQF NWGLDNTICI KLQNVVHVLK YERLEQRYPI ENSYTFSVPL IDTNCKCHCY
GFGTNDVCNV EKYADDRNCT TSSEFPTCYT KYHPAVEPLD CPVTSIPAKA CCDIKLKPRD
GRMFRAVKLQ QPINDMIISH SIFANNSGKM MKVLGPDEFR INLLKGKEQF ELTEYHRISV
QLVASSPQQQ LREGMYYFPE ENHNDLREGK INEITESDLD KLGWYRRVGN DWQVATSGLL
LRNAHKVVIK NCKGQVHMDQ FSGTKNFVLR GTQYNDTYNE RRVSDNNFVR SVKVDESSRE
ITIVHEHGTA AQVSLKTDTR PNLTKSQSLL ANFTGSITLD HDGNRMLNVT FFGVKGTVHI
KMYVNDRKLI ATFACTAQFG TSLKDDGSRI SLPSTINQAQ WVCILPDEQP TKSEICKWIP
YEEKAMRTPR QEQSWSKGHS PCSQAECNSL KSGVSDLFPW IMNFDYFMAH GGDFTEWLKI
GIHIVIAVGL LLLLILLFTK CLVPLACCSL SIPFKNRNKK KKKKNSSDY
