EQTN_MOUSE
ID EQTN_MOUSE Reviewed; 337 AA.
AC Q9D9V2; A2AJE0; Q2LCV5; Q5FWB0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Equatorin;
DE AltName: Full=Acrosome formation-associated factor;
DE AltName: Full=MN9 antigen;
DE Flags: Precursor;
GN Name=Eqtn; Synonyms=Afaf, Mn9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=16831425; DOI=10.1016/j.febslet.2006.06.010;
RA Li Y.-C., Hu X.-Q., Zhang K.-Y., Guo J., Hu Z.-Y., Tao S.-X., Xiao L.-J.,
RA Wang Q.-Z., Han C.-S., Liu Y.-X.;
RT "Afaf, a novel vesicle membrane protein, is related to acrosome formation
RT in murine testis.";
RL FEBS Lett. 580:4266-4273(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=9674989; DOI=10.1095/biolreprod59.1.22;
RA Toshimori K., Saxena D.K., Tanii I., Yoshinaga K.;
RT "An MN9 antigenic molecule, equatorin, is required for successful sperm-
RT oocyte fusion in mice.";
RL Biol. Reprod. 59:22-29(1998).
RN [6]
RP CHARACTERIZATION OF THE EPITOPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, MUTAGENESIS OF THR-128; SER-129; THR-130; THR-138 AND
RP SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19605790; DOI=10.1095/biolreprod.109.077438;
RA Yamatoya K., Yoshida K., Ito C., Maekawa M., Yanagida M., Takamori K.,
RA Ogawa H., Araki Y., Miyado K., Toyama Y., Toshimori K.;
RT "Equatorin: identification and characterization of the epitope of the MN9
RT antibody in the mouse.";
RL Biol. Reprod. 81:889-897(2009).
RN [7]
RP INTERACTION WITH SNAP25, AND FUNCTION.
RX PubMed=19285662; DOI=10.1016/j.fertnstert.2009.01.067;
RA Hu X.Q., Ji S.Y., Li Y.C., Fan C.H., Cai H., Yang J.L., Zhang C.P.,
RA Chen M., Pan Z.F., Hu Z.Y., Gao F., Liu Y.X.;
RT "Acrosome formation-associated factor is involved in fertilization.";
RL Fertil. Steril. 93:1482-1492(2010).
CC -!- FUNCTION: Acrosomal membrane-anchored protein involved in the process
CC of fertilization and in acrosome biogenesis.
CC {ECO:0000269|PubMed:16831425, ECO:0000269|PubMed:19285662,
CC ECO:0000269|PubMed:9674989}.
CC -!- SUBUNIT: Interacts with SNAP25. {ECO:0000269|PubMed:19285662}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome membrane; Single-pass type I membrane protein.
CC Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane;
CC Single-pass type I membrane protein. Cytoplasmic vesicle, secretory
CC vesicle, acrosome outer membrane; Single-pass type I membrane protein.
CC Note=In the anterior acrosome region, enriched on the inner acrosomal
CC membrane but minimal on the outer acrosomal membrane; in contrast in
CC the posterior acrosome region enriched on both the inner and outer
CC acrosomal membranes.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9V2-2; Sequence=VSP_025111;
CC -!- TISSUE SPECIFICITY: Sperm specific, including germ cells (at protein
CC level). {ECO:0000269|PubMed:16831425, ECO:0000269|PubMed:19605790}.
CC -!- PTM: Highly N- and O-glycosylated; contains sialic acid. MN9 epitope is
CC O-glycosylated. {ECO:0000269|PubMed:19605790}.
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DR EMBL; DQ336137; ABC69297.1; -; mRNA.
DR EMBL; AK006446; BAB24593.1; -; mRNA.
DR EMBL; AL732611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089517; AAH89517.1; -; mRNA.
DR CCDS; CCDS18362.1; -. [Q9D9V2-1]
DR CCDS; CCDS71422.1; -. [Q9D9V2-2]
DR RefSeq; NP_001277552.1; NM_001290623.1. [Q9D9V2-2]
DR RefSeq; NP_081365.2; NM_027089.4. [Q9D9V2-1]
DR AlphaFoldDB; Q9D9V2; -.
DR SMR; Q9D9V2; -.
DR STRING; 10090.ENSMUSP00000030309; -.
DR GlyGen; Q9D9V2; 1 site.
DR PhosphoSitePlus; Q9D9V2; -.
DR PaxDb; Q9D9V2; -.
DR PRIDE; Q9D9V2; -.
DR ProteomicsDB; 275876; -. [Q9D9V2-1]
DR ProteomicsDB; 275877; -. [Q9D9V2-2]
DR Antibodypedia; 2383; 23 antibodies from 12 providers.
DR Ensembl; ENSMUST00000030309; ENSMUSP00000030309; ENSMUSG00000028575. [Q9D9V2-1]
DR Ensembl; ENSMUST00000107097; ENSMUSP00000102714; ENSMUSG00000028575. [Q9D9V2-2]
DR GeneID; 67753; -.
DR KEGG; mmu:67753; -.
DR UCSC; uc008tsl.3; mouse. [Q9D9V2-2]
DR UCSC; uc008tsm.2; mouse. [Q9D9V2-1]
DR CTD; 54586; -.
DR MGI; MGI:1915003; Eqtn.
DR VEuPathDB; HostDB:ENSMUSG00000028575; -.
DR eggNOG; KOG2248; Eukaryota.
DR GeneTree; ENSGT00390000010786; -.
DR HOGENOM; CLU_082439_0_0_1; -.
DR InParanoid; Q9D9V2; -.
DR OMA; GPNEPAF; -.
DR OrthoDB; 1090314at2759; -.
DR PhylomeDB; Q9D9V2; -.
DR TreeFam; TF337449; -.
DR BioGRID-ORCS; 67753; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Eqtn; mouse.
DR PRO; PR:Q9D9V2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D9V2; protein.
DR Bgee; ENSMUSG00000028575; Expressed in spermatid and 28 other tissues.
DR Genevisible; Q9D9V2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0002079; C:inner acrosomal membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0002081; C:outer acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IMP:MGI.
DR GO; GO:0001675; P:acrosome assembly; TAS:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:MGI.
DR InterPro; IPR029282; Eqtn/Afaf.
DR PANTHER; PTHR36874; PTHR36874; 1.
DR Pfam; PF15339; Afaf; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..337
FT /note="Equatorin"
FT /id="PRO_0000286594"
FT TOPO_DOM 21..183
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2LCV6"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 239..279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16831425"
FT /id="VSP_025111"
FT MUTAGEN 128
FT /note="T->A: Does not affect MN9 antibody detectability."
FT /evidence="ECO:0000269|PubMed:19605790"
FT MUTAGEN 129
FT /note="S->A: Does not affect MN9 antibody detectability."
FT /evidence="ECO:0000269|PubMed:19605790"
FT MUTAGEN 130
FT /note="T->A: Does not affect MN9 antibody detectability."
FT /evidence="ECO:0000269|PubMed:19605790"
FT MUTAGEN 138
FT /note="T->A: MN9 antibody detectability is lost."
FT /evidence="ECO:0000269|PubMed:19605790"
FT MUTAGEN 141
FT /note="S->A: Does not affect MN9 antibody detectability."
FT /evidence="ECO:0000269|PubMed:19605790"
FT CONFLICT 214
FT /note="R -> S (in Ref. 1; ABC69297 and 2; BAB24593)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="A -> H (in Ref. 1; ABC69297 and 2; BAB24593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37764 MW; 3F2103B1EFD10F61 CRC64;
MDFILLIILS GVFLPDIISL QPIVGQEPGV TLSDEEQYYA DEENNTDGNS VALHKLEENE
MDTPANEKTG NYYKDIKQYV FTTPNIKGSE VSVTATTNLE FAVKKNYKAS KPTASGEEEK
PSESSRKTST PNIPAFWTIL SKAVNETAVS MDDKDQFFQP IPASDLNATN EDKLSELEEI
KLKLMLGISL MTLVLLIPLL IFCFATLYKL RHLRDKSYES QYSINPELAT LSYFHPTEGV
SDTSFSKSAD SNSYWVHNSS EMRRSRTRRS KSKPMDFSAG SNQTVLTDES SFLPPEETRF
LLPEEPGKEL IVERGPMQAM NEIDAQLLLN KEGSPSN
