ID   SPAT2_RAT               Reviewed;         511 AA.
AC   Q66HP6; F1LNA7; Q91XS7;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Spermatogenesis-associated protein 2 {ECO:0000305};
GN   Name=Spata2 {ECO:0000312|RGD:620754};
GN   Synonyms=Pd1 {ECO:0000303|PubMed:11079456};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   TISSUE=Testis;
RX   PubMed=11322771; DOI=10.1006/bbrc.2001.4754;
RA   Onisto M., Slongo L.M., Graziotto R., Zotti L., Negro A., Merico M.,
RA   Moro E., Foresta C., Maurizio O., Liliana S.M., Romina G., Lorenza Z.,
RA   Alessandro N., Maurizio M., Enrico M., Carlo F.;
RT   "Evidence for FSH-dependent upregulation of SPATA2 (spermatogenesis-
RT   associated protein 2).";
RL   Biochem. Biophys. Res. Commun. 283:86-92(2001).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11079456; DOI=10.1007/bf03343783;
RA   Onisto M., Graziotto R., Scannapieco P., Marin P., Merico M., Slongo M.L.,
RA   Foresta C.;
RT   "A novel gene (PD1) with a potential role on rat spermatogenesis.";
RL   J. Endocrinol. Invest. 23:605-608(2000).
CC   -!- FUNCTION: Bridging factor that mediates the recruitment of CYLD to the
CC       LUBAC complex, thereby regulating TNF-alpha-induced necroptosis. Acts
CC       as a direct binding intermediate that bridges RNF31/HOIP, the catalytic
CC       subunit of the LUBAC complex, and the deubiquitinase (CYLD), thereby
CC       recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC). Required to
CC       activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase
CC       activities of CYLD (By similarity). Controls the kinase activity of
CC       RIPK1 and TNF-alpha-induced necroptosis by promoting 'Met-1'-linked
CC       deubiquitination of RIPK1 by CYLD (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K004, ECO:0000250|UniProtKB:Q9UM82}.
CC   -!- SUBUNIT: Interacts (via the PIM motif) with RNF31/HOIP (via the PUB
CC       domain); the interaction is direct. Interacts (via the PUB domain) with
CC       CYLD; the interaction is direct. {ECO:0000250|UniProtKB:Q9UM82}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UM82}. Nucleus
CC       {ECO:0000269|PubMed:11322771}.
CC   -!- TISSUE SPECIFICITY: Expressed in the testis and to a lesser extent in
CC       the brain, while skeletal muscle and kidney show weak expression.
CC       {ECO:0000269|PubMed:11079456, ECO:0000269|PubMed:11322771}.
CC   -!- DEVELOPMENTAL STAGE: During testicular development (from 2 to 45 days
CC       of age), expressed from 14 days and then increases steadily with an
CC       advancement of age. {ECO:0000269|PubMed:11079456}.
CC   -!- INDUCTION: Up-regulated following FSH treatment.
CC       {ECO:0000269|PubMed:11322771}.
CC   -!- SIMILARITY: Belongs to the SPATA2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK61814.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF123651; AAK61814.1; ALT_INIT; mRNA.
DR   EMBL; AC131854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC081752; AAH81752.1; -; mRNA.
DR   EMBL; CH474005; EDL96405.1; -; Genomic_DNA.
DR   PIR; JC7682; JC7682.
DR   RefSeq; NP_446127.3; NM_053675.2.
DR   RefSeq; XP_006235698.1; XM_006235636.3.
DR   AlphaFoldDB; Q66HP6; -.
DR   SMR; Q66HP6; -.
DR   STRING; 10116.ENSRNOP00000012604; -.
DR   PaxDb; Q66HP6; -.
DR   PRIDE; Q66HP6; -.
DR   Ensembl; ENSRNOT00000012604; ENSRNOP00000012604; ENSRNOG00000009207.
DR   GeneID; 114210; -.
DR   KEGG; rno:114210; -.
DR   CTD; 9825; -.
DR   RGD; 620754; Spata2.
DR   eggNOG; ENOG502RR2T; Eukaryota.
DR   GeneTree; ENSGT00530000063956; -.
DR   HOGENOM; CLU_039585_0_0_1; -.
DR   InParanoid; Q66HP6; -.
DR   OMA; RTHLAKE; -.
DR   OrthoDB; 461395at2759; -.
DR   PhylomeDB; Q66HP6; -.
DR   TreeFam; TF328840; -.
DR   PRO; PR:Q66HP6; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Proteomes; UP000234681; Chromosome 3.
DR   Bgee; ENSRNOG00000009207; Expressed in jejunum and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:RGD.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR   GO; GO:0070266; P:necroptotic process; ISO:RGD.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990108; P:protein linear deubiquitination; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0060544; P:regulation of necroptotic process; ISS:UniProtKB.
DR   GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR   InterPro; IPR029744; SPATA2.
DR   PANTHER; PTHR15326:SF8; PTHR15326:SF8; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Necrosis; Nucleus; Reference proteome.
FT   CHAIN           1..511
FT                   /note="Spermatogenesis-associated protein 2"
FT                   /id="PRO_0000445575"
FT   DOMAIN          77..149
FT                   /note="PUB"
FT                   /evidence="ECO:0000255"
FT   MOTIF           320..337
FT                   /note="PIM motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM82"
FT   CONFLICT        172
FT                   /note="I -> M (in Ref. 1; AAK61814)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="K -> E (in Ref. 1; AAK61814)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="P -> L (in Ref. 1; AAK61814)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  57481 MW;  2193C37426023CE5 CRC64;
     MDTKYKDDLF RKYVQFHEGK VDTTPGKQSG SDEYLRVAAA TLLSLHKVDP LYRFRLIQFY
     EVVESSLRSL SSSSLSALHC AFSMLETMAI NLFLFPWKKE FRSIKTYTGP FVYYVKSTLL
     EKDIRAILKF MGYEPELGTA YKLKELVESL QVKMVSFELF LAKVECEQML GIHSQVKDKG
     YSELDVVTER KSSTEDARGC SDALRRRAES REHLTTSMAR VALQKSASER AAKDYYKPRV
     TKPSRSVDAY DSYWESRKPP SKASLSLRKE PLAMDVGEDL KDEIIRPSPS LLTMSSSPHG
     SPDDLPSISP INGLGLLRST YFPTQDDVDL YTDSEPRATY RRQDALRSDI WLVKNDAHSI
     YHKRSPPTKE SALSKCQNCG LSCSSSLCQR CDSVCPSASK PSGFPSKASA HDSLVHGAPM
     REKYVGQTQG LDRLATVHSK PKPSTTATSR CGFCNRAGAT NTCTQCSKVS CDPCLGAYHY
     DPCCRKSELH KFMPNNQLNY KSTQFSHPVY R