SPE9_CAEEL
ID SPE9_CAEEL Reviewed; 661 AA.
AC Q9TVY6; B3WFX0; O61537; Q8MLX3; Q8MM25; Q8MV49; Q8MV50; Q8MV51; Q8MV52;
AC Q8MV53; Q8MV54;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sperm transmembrane protein 9;
DE AltName: Full=Fertilization defective 9;
DE AltName: Full=Spermatogenesis defective 9;
DE Flags: Precursor;
GN Name=spe-9; ORFNames=C17D12.6;
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:0000305, ECO:0000312|EMBL:AAC38980.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND MUTAGENESIS OF
RP CYS-258 AND GLY-550.
RX PubMed=9546393; DOI=10.1016/s0092-8674(00)81147-2;
RA Singson A., Mercer K.B., L'Hernault S.W.;
RT "The C. elegans spe-9 gene encodes a sperm transmembrane protein that
RT contains EGF-like repeats and is required for fertilization.";
RL Cell 93:71-79(1998).
RN [2] {ECO:0000312|EMBL:CAB60992.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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] {ECO:0000269|PubMed:12019226, ECO:0000305, ECO:0000312|EMBL:AAM49739.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-661.
RC STRAIN=AB1 {ECO:0000269|PubMed:12019226},
RC AB2 {ECO:0000312|EMBL:AAM49741.1},
RC Bristol N2 {ECO:0000312|EMBL:AAM49739.1},
RC CB4507 {ECO:0000269|PubMed:12019226}, CB4851 {ECO:0000269|PubMed:12019226},
RC CB4852 {ECO:0000269|PubMed:12019226}, CB4853 {ECO:0000312|EMBL:AAM49744.1},
RC CB4854 {ECO:0000269|PubMed:12019226}, CB4855 {ECO:0000312|EMBL:AAM49746.1},
RC CB4856 {ECO:0000269|PubMed:12019226}, CB4857 {ECO:0000312|EMBL:AAM49748.1},
RC CB4858 {ECO:0000312|EMBL:AAM49749.1}, CB4932 {ECO:0000269|PubMed:12019226},
RC DH424 {ECO:0000312|EMBL:AAM49751.1}, DR1344 {ECO:0000269|PubMed:12019226},
RC PB303 {ECO:0000269|PubMed:12019226}, PB305 {ECO:0000269|PubMed:12019226},
RC PB306 {ECO:0000269|PubMed:12019226}, PB307 {ECO:0000269|PubMed:12019226},
RC and TR388 {ECO:0000269|PubMed:12019226};
RX PubMed=12019226; DOI=10.1093/genetics/161.1.99;
RA Graustein A., Gaspar J.M., Walters J.R., Palopoli M.F.;
RT "Levels of DNA polymorphism vary with mating system in the nematode genus
RT Caenorhabditis.";
RL Genetics 161:99-107(2002).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14653860; DOI=10.1186/1471-213x-3-10;
RA Zannoni S., L'Hernault S.W., Singson A.W.;
RT "Dynamic localization of SPE-9 in sperm: a protein required for sperm-
RT oocyte interactions in Caenorhabditis elegans.";
RL BMC Dev. Biol. 3:10-10(2003).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-258 AND GLY-550.
RX PubMed=15282160; DOI=10.1016/j.ydbio.2004.05.014;
RA Putiri E., Zannoni S., Kadandale P., Singson A.;
RT "Functional domains and temperature-sensitive mutations in SPE-9, an EGF
RT repeat-containing protein required for fertility in Caenorhabditis
RT elegans.";
RL Dev. Biol. 272:448-459(2004).
CC -!- FUNCTION: Required for fertilization. May be required for cell adhesion
CC and/or function as a signaling molecule. {ECO:0000269|PubMed:15282160,
CC ECO:0000269|PubMed:9546393}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14653860,
CC ECO:0000305}. Membrane {ECO:0000269|PubMed:14653860, ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:14653860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9546393};
CC IsoId=Q9TVY6-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TVY6-2; Sequence=VSP_053190;
CC -!- TISSUE SPECIFICITY: Expressed in spermatids, during spermogenesis
CC expression is primarily localized to the pseudopod.
CC {ECO:0000269|PubMed:14653860, ECO:0000269|PubMed:15282160}.
CC -!- MISCELLANEOUS: Removing the EGF-like repeats in any combination
CC completely abolishes fertilization. {ECO:0000269|PubMed:15282160}.
CC -!- MISCELLANEOUS: Modifying each EGF repeat by changing a central cysteine
CC residue to a tyrosine disrupts the secondary structure as the specific
CC disulfide bridges responsible for this overall structure are not
CC formed. The cysteine to tyrosine mutation when located in EGF-like
CC domains 1,3,4 and 5, causes a complete loss of function. The same
CC mutation in additional EGF-like domains leads to a temperature
CC sensitive sterile phenotype. {ECO:0000269|PubMed:15282160,
CC ECO:0000269|PubMed:9546393}.
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DR EMBL; AF049327; AAC38980.1; -; mRNA.
DR EMBL; Z81473; CAB60992.2; -; Genomic_DNA.
DR EMBL; Z81063; CAB60992.2; JOINED; Genomic_DNA.
DR EMBL; Z81473; CAQ76456.1; -; Genomic_DNA.
DR EMBL; Z81063; CAQ76456.1; JOINED; Genomic_DNA.
DR EMBL; AF492686; AAM49739.1; -; Genomic_DNA.
DR EMBL; AF492687; AAM49740.1; -; Genomic_DNA.
DR EMBL; AF492688; AAM49741.1; -; Genomic_DNA.
DR EMBL; AF492690; AAM49742.1; -; Genomic_DNA.
DR EMBL; AF492691; AAM49743.1; -; Genomic_DNA.
DR EMBL; AF492692; AAM49744.1; -; Genomic_DNA.
DR EMBL; AF492693; AAM49745.1; -; Genomic_DNA.
DR EMBL; AF492694; AAM49746.1; -; Genomic_DNA.
DR EMBL; AF492695; AAM49747.1; -; Genomic_DNA.
DR EMBL; AF492696; AAM49748.1; -; Genomic_DNA.
DR EMBL; AF492697; AAM49749.1; -; Genomic_DNA.
DR EMBL; AF492698; AAM49750.1; -; Genomic_DNA.
DR EMBL; AF492699; AAM49751.1; -; Genomic_DNA.
DR EMBL; AF492700; AAM49752.1; -; Genomic_DNA.
DR EMBL; AF492701; AAM49753.1; -; Genomic_DNA.
DR PIR; T42754; T42754.
DR RefSeq; NP_001129750.1; NM_001136278.1. [Q9TVY6-2]
DR RefSeq; NP_492955.1; NM_060554.4. [Q9TVY6-1]
DR AlphaFoldDB; Q9TVY6; -.
DR BioGRID; 38449; 8.
DR STRING; 6239.C17D12.6a; -.
DR PaxDb; Q9TVY6; -.
DR EnsemblMetazoa; C17D12.6a.1; C17D12.6a.1; WBGene00004963. [Q9TVY6-1]
DR EnsemblMetazoa; C17D12.6b.1; C17D12.6b.1; WBGene00004963. [Q9TVY6-2]
DR GeneID; 173042; -.
DR KEGG; cel:CELE_C17D12.6; -.
DR UCSC; C17D12.6; c. elegans.
DR CTD; 173042; -.
DR WormBase; C17D12.6a; CE27074; WBGene00004963; spe-9. [Q9TVY6-1]
DR WormBase; C17D12.6b; CE42755; WBGene00004963; spe-9. [Q9TVY6-2]
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_027231_0_0_1; -.
DR InParanoid; Q9TVY6; -.
DR OMA; NYWWTYP; -.
DR OrthoDB; 388074at2759; -.
DR PhylomeDB; Q9TVY6; -.
DR PRO; PR:Q9TVY6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004963; Expressed in larva and 1 other tissue.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0031143; C:pseudopodium; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; ISS:WormBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IMP:WormBase.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 4.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cytoplasm; Disulfide bond;
KW EGF-like domain; Fertilization; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..661
FT /note="Sperm transmembrane protein 9"
FT /evidence="ECO:0000269|PubMed:15282160"
FT /id="PRO_0000391385"
FT TOPO_DOM 17..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..90
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 210..259
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 377..414
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 519..557
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 559..600
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOTIF 377..379
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 214..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 219..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 385..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 393..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 528..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 547..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 563..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 571..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 590..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12019226"
FT /id="VSP_053190"
FT MUTAGEN 258
FT /note="C->Y: Disrupts formation of specific disulfide
FT bridges resulting in loss of function."
FT /evidence="ECO:0000269|PubMed:15282160,
FT ECO:0000269|PubMed:9546393"
FT MUTAGEN 550
FT /note="G->E: Temperature sensitive for fertility. Wild-type
FT levels of fertility between 16 and 20 degrees Celsius, at
FT 25 degrees Celsius fertility levels drop drastically."
FT /evidence="ECO:0000269|PubMed:15282160,
FT ECO:0000269|PubMed:9546393"
FT CONFLICT 47
FT /note="V -> L (in Ref. 3; AAM49747)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> T (in Ref. 3; AAM49747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 73600 MW; 8AAFDEC67184AD6E CRC64;
MNVILVLVVL FFAGDCAKIR KIIDFLEKDA PNDIEKTPNY NEESLAVKRN KNFNPCLENP
KICSNRGKCL HENGNFYCIC PVTHYGKTCE HVSDQTNCEK HLCQNNSTCV SIKSLRTIVN
TVLLRQIRVQ RKVNGSKAAL TNEELAEIDL EVNYECICQK GYFGGLCDES EADRTCQEVY
CLGRGKGAIN ATGKCECECE NQFFGDRCEQ ISACFDTQCD NGGICEDVVD WKTKTVTATC
KCPSAIELIG GTVTGENCET LQIPSTAPKE FIPCAEGSNS TMFFKKFIAN ISLEYMDDIS
ELEAIKNDYN DGKNVNGTMT DGWCRNDGKC VPEVVRVNSS RAYYIYRCEC TNPLTDGYYC
EYKRHDSCSL TREEVARGDR WDEKCTDSQH GACVDISGVA HCVCKPDYTG EKCEIFDPCA
RQPCKHGDCI PIPNTADVAF GTSRYQCLCP LSAKLNPESQ ACMEINEKKC APGACGNGRC
VPCESDADDL MPLCNDNDNR QGFRCLCEAG YLPPFCKVHT NPCYQNLCQN SATCHIDPKQ
RSYDCQCVNG TRGSLCENVD DSCDAFGNKI CVHGTCINDE YFHRGFSCEC DDGFEGLDCN
VEIAWSSVMT NRLMKNYEFS LPLVACFVSL AILLPVIVIS RRRQGRVEEA KKTSEVKTEN
P
