ID   EQTN_RAT                Reviewed;         280 AA.
AC   Q2LCV6; F1LP31;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Equatorin;
DE   AltName: Full=Acrosome formation-associated factor;
DE   Flags: Precursor;
GN   Name=Eqtn; Synonyms=Afaf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; 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 GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Acrosomal membrane-anchored protein involved in the process
CC       of fertilization and in acrosome biogenesis. {ECO:0000250,
CC       ECO:0000269|PubMed:16831425}.
CC   -!- SUBUNIT: Interacts with SNAP25. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       membrane; Single-pass type I membrane protein. Cytoplasmic vesicle,
CC       secretory vesicle, acrosome inner membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory
CC       vesicle, acrosome outer membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=In the anterior acrosome region,
CC       enriched on the inner acrosomal membrane but minimal on the outer
CC       acrosomal membrane; in contrast in the posterior acrosome region
CC       enriched on both the inner and outer acrosomal membranes.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and epididymis. Low
CC       expression in other tissues. {ECO:0000269|PubMed:16831425}.
CC   -!- PTM: Highly N- and O-glycosylated; contains sialic acid. {ECO:0000250}.
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DR   EMBL; DQ336136; ABC69296.1; -; mRNA.
DR   EMBL; AABR06038744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001034434.1; NM_001039345.1.
DR   RefSeq; XP_017449065.1; XM_017593576.1.
DR   AlphaFoldDB; Q2LCV6; -.
DR   SMR; Q2LCV6; -.
DR   STRING; 10116.ENSRNOP00000034172; -.
DR   GlyGen; Q2LCV6; 1 site.
DR   iPTMnet; Q2LCV6; -.
DR   PhosphoSitePlus; Q2LCV6; -.
DR   PaxDb; Q2LCV6; -.
DR   GeneID; 500502; -.
DR   KEGG; rno:500502; -.
DR   UCSC; RGD:1563332; rat.
DR   CTD; 54586; -.
DR   RGD; 1563332; Eqtn.
DR   VEuPathDB; HostDB:ENSRNOG00000026323; -.
DR   eggNOG; KOG2248; Eukaryota.
DR   HOGENOM; CLU_082439_0_0_1; -.
DR   InParanoid; Q2LCV6; -.
DR   OMA; GPNEPAF; -.
DR   OrthoDB; 1090314at2759; -.
DR   TreeFam; TF337449; -.
DR   PRO; PR:Q2LCV6; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000026323; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0002079; C:inner acrosomal membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0002081; C:outer acrosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:RGD.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISO:RGD.
DR   InterPro; IPR029282; Eqtn/Afaf.
DR   PANTHER; PTHR36874; PTHR36874; 1.
DR   Pfam; PF15339; Afaf; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..280
FT                   /note="Equatorin"
FT                   /id="PRO_0000286595"
FT   TOPO_DOM        20..183
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          112..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        27
FT                   /note="D -> G (in Ref. 1; ABC69296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  31388 MW;  322F245087A00AF2 CRC64;
     MDFILLIFLS GVFLPNIFSL QPTVEQDPGV TISDDQYYDE EENNTDENSA IFQKLEDNGG
     DTPANEKTGN YYKDIKQYVF TTPDSKGTKT EVSVTATTDL KFTMKDYKSS KATASGEEDK
     RSEPSRKSST PNVPAFWTML AKAINETAVS MDDKDLFYQA IPASDLNSTN EDQLSELEEI
     KLKLMLGISL MTLILLIPLL IFCFATLYKL RHLRDKTCES QYSVNPELAT LSYFHPSEGS
     NQTVLTEESS FLPPEESGKV VIIESNTVNE AEVTEERISE