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Cell fusion protein aff-1 (Anchor cell fusion failure protein 1)

 AFF1_CAEEL              Reviewed;         589 AA.
G5EGL9;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
10-OCT-2018, entry version 48.
RecName: Full=Cell fusion protein aff-1 {ECO:0000305|PubMed:17488621};
AltName: Full=Anchor cell fusion failure protein 1 {ECO:0000312|EMBL:ABP04049.1};
Flags: Precursor;
Name=aff-1 {ECO:0000312|WormBase:C44B7.3};
ORFNames=C44B7.3 {ECO:0000312|WormBase:C44B7.3};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000312|EMBL:ABP04049.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=17488621; DOI=10.1016/j.devcel.2007.03.003;
Sapir A., Choi J., Leikina E., Avinoam O., Valansi C.,
Chernomordik L.V., Newman A.P., Podbilewicz B.;
"AFF-1, a FOS-1-regulated fusogen, mediates fusion of the anchor cell
in C. elegans.";
Dev. Cell 12:683-698(2007).
[2] {ECO:0000312|EMBL:CCD61566.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD61566.1};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=21350017; DOI=10.1242/dev.058305;
Procko C., Lu Y., Shaham S.;
"Glia delimit shape changes of sensory neuron receptive endings in C.
elegans.";
Development 138:1371-1381(2011).
-!- FUNCTION: Required for cell fusion events during development
including the fusion of anchor cells (AC), vulval A and vulval D
rings, and late epidermal seam cells (PubMed:17488621). Required
for amphid sheath cell fusion induced by entry into dauer stage
(PubMed:21350017). {ECO:0000269|PubMed:17488621,
ECO:0000269|PubMed:21350017}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17488621};
Single-pass type I membrane protein {ECO:0000255}. Apical cell
membrane {ECO:0000269|PubMed:21350017}.
-!- TISSUE SPECIFICITY: Expressed in amphid sheath cells.
{ECO:0000269|PubMed:21350017}.
-!- DEVELOPMENTAL STAGE: First expressed in embryonic hyp5 cells and
then during larval development in pharyngeal muscles, uterine
rings, head and tail neurons, sheath cells of chemo-sensory
neurons, and in male neurons. Expressed in AC, vulval D rings and
uterine seam cells in cell fusion events during development.
{ECO:0000269|PubMed:17488621}.
-!- DISRUPTION PHENOTYPE: Egg laying defective phenotype. AC fail to
fuse in the majority of worms (PubMed:17488621). RNAi-mediated
knockdown in a daf-7 e1372 mutant background causes a severe
defect in amphid sheath cell fusion induced by entry into dauer
stage (PubMed:21350017). {ECO:0000269|PubMed:17488621,
ECO:0000269|PubMed:21350017}.
-!- SIMILARITY: Belongs to the EFF/AFF cell fusogen family.
{ECO:0000305}.
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EMBL; EF205023; ABP04049.1; -; mRNA.
EMBL; FO080141; CCD61566.1; -; Genomic_DNA.
RefSeq; NP_495402.3; NM_063001.5.
UniGene; Cel.7622; -.
ProteinModelPortal; G5EGL9; -.
STRING; 6239.C44B7.3; -.
TCDB; 1.N.4.1.4; the ff fusogen (fff) family.
PaxDb; G5EGL9; -.
EnsemblMetazoa; C44B7.3; C44B7.3; WBGene00016625.
GeneID; 174123; -.
KEGG; cel:CELE_C44B7.3; -.
CTD; 174123; -.
WormBase; C44B7.3; CE41369; WBGene00016625; aff-1.
eggNOG; ENOG410K7BQ; Eukaryota.
eggNOG; ENOG4110MJJ; LUCA.
GeneTree; ENSGT00390000003363; -.
InParanoid; G5EGL9; -.
OMA; TEYHRIS; -.
OrthoDB; EOG091G03CE; -.
PhylomeDB; G5EGL9; -.
PRO; PR:G5EGL9; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00016625; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0007275; P:multicellular organism development; IGI:WormBase.
GO; GO:0045026; P:plasma membrane fusion; IBA:GO_Central.
GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IMP:WormBase.
InterPro; IPR029213; Fusogen_EFF/AFF.
PANTHER; PTHR37415; PTHR37415; 1.
Pfam; PF14884; EFF-AFF; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Developmental protein; Glycoprotein;
Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 589 Cell fusion protein aff-1. {ECO:0000255}.
/FTId=PRO_0000432857.
TOPO_DOM 21 537 Extracellular. {ECO:0000305}.
TRANSMEM 538 558 Helical. {ECO:0000255}.
TOPO_DOM 559 589 Cytoplasmic. {ECO:0000305}.
COMPBIAS 579 584 Poly-Lys. {ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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


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