HORM2_MOUSE
ID HORM2_MOUSE Reviewed; 306 AA.
AC Q5SQP1; B7ZMW2; Q9D507;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=HORMA domain-containing protein 2;
GN Name=Hormad2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19851446; DOI=10.1371/journal.pgen.1000702;
RA Wojtasz L., Daniel K., Roig I., Bolcun-Filas E., Xu H., Boonsanay V.,
RA Eckmann C.R., Cooke H.J., Jasin M., Keeney S., McKay M.J., Toth A.;
RT "Mouse HORMAD1 and HORMAD2, two conserved meiotic chromosomal proteins, are
RT depleted from synapsed chromosome axes with the help of TRIP13 AAA-
RT ATPase.";
RL PLoS Genet. 5:E1000702-E1000702(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23039116; DOI=10.1111/gtc.12005;
RA Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.;
RT "HORMAD2 is essential for synapsis surveillance during meiotic prophase via
RT the recruitment of ATR activity.";
RL Genes Cells 17:897-912(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP HORMAD1.
RX PubMed=22549958; DOI=10.1101/gad.187559.112;
RA Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J.,
RA Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.;
RT "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
RT monitored by distinct HORMAD2-independent and -dependent mechanisms.";
RL Genes Dev. 26:958-973(2012).
RN [8]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
CC -!- FUNCTION: Essential for synapsis surveillance during meiotic prophase
CC via the recruitment of ATR activity. Plays a key role in the male mid-
CC pachytene checkpoint and the female meiotic prophase checkpoint:
CC required for efficient build-up of ATR activity on unsynapsed
CC chromosome regions, a process believed to form the basis of meiotic
CC silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality
CC control in both sexes. Required for the DNA double-strand break-
CC independent, BRCA1-dependent activation of ATR on the sex chromosomes
CC that is essential for normal sex body formation.
CC {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116}.
CC -!- SUBUNIT: Interacts with HORMAD1. {ECO:0000269|PubMed:22549958}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Preferentially
CC localizes to unsynapsed or desynapsed chromosomal regions during the
CC male and female prophase I stage of meiosis. TRIP13 is required for
CC depletion from synapsed chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SQP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SQP1-2; Sequence=VSP_024605, VSP_024606;
CC -!- TISSUE SPECIFICITY: Specifically expressed in meiotic germ cells.
CC {ECO:0000269|PubMed:19851446}.
CC -!- PTM: Phosphorylated in a SPO11-dependent manner.
CC {ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:23039116}.
CC -!- DISRUPTION PHENOTYPE: Male mice are infertile due to spermatocyte loss
CC as a result of characteristic impairment of sex body formation.
CC Spermatocyte apoptosis is confined to the stage IV seminiferous
CC tubules. In contrast to males, female mice are fertile.
CC {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116}.
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DR EMBL; AK015939; BAB30043.1; -; mRNA.
DR EMBL; AL645910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120781; AAI20782.1; -; mRNA.
DR EMBL; BC120783; AAI20784.1; -; mRNA.
DR EMBL; BC144842; AAI44843.1; -; mRNA.
DR CCDS; CCDS36096.1; -. [Q5SQP1-1]
DR RefSeq; NP_083734.1; NM_029458.1. [Q5SQP1-1]
DR RefSeq; XP_011242079.1; XM_011243777.2. [Q5SQP1-1]
DR RefSeq; XP_011242081.1; XM_011243779.2. [Q5SQP1-1]
DR RefSeq; XP_011242082.1; XM_011243780.2. [Q5SQP1-1]
DR RefSeq; XP_011242083.1; XM_011243781.1. [Q5SQP1-1]
DR AlphaFoldDB; Q5SQP1; -.
DR SMR; Q5SQP1; -.
DR STRING; 10090.ENSMUSP00000105574; -.
DR iPTMnet; Q5SQP1; -.
DR PhosphoSitePlus; Q5SQP1; -.
DR PaxDb; Q5SQP1; -.
DR PRIDE; Q5SQP1; -.
DR ProteomicsDB; 273380; -. [Q5SQP1-1]
DR ProteomicsDB; 273381; -. [Q5SQP1-2]
DR Antibodypedia; 311; 146 antibodies from 19 providers.
DR Ensembl; ENSMUST00000109948; ENSMUSP00000105574; ENSMUSG00000020419. [Q5SQP1-1]
DR Ensembl; ENSMUST00000109949; ENSMUSP00000105575; ENSMUSG00000020419. [Q5SQP1-1]
DR GeneID; 75828; -.
DR KEGG; mmu:75828; -.
DR UCSC; uc007huv.1; mouse. [Q5SQP1-1]
DR UCSC; uc011xqw.1; mouse. [Q5SQP1-2]
DR CTD; 150280; -.
DR MGI; MGI:1923078; Hormad2.
DR VEuPathDB; HostDB:ENSMUSG00000020419; -.
DR eggNOG; KOG4652; Eukaryota.
DR GeneTree; ENSGT00390000018130; -.
DR HOGENOM; CLU_058638_2_0_1; -.
DR InParanoid; Q5SQP1; -.
DR OMA; YLQIVFI; -.
DR OrthoDB; 1038689at2759; -.
DR PhylomeDB; Q5SQP1; -.
DR TreeFam; TF313989; -.
DR BioGRID-ORCS; 75828; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hormad2; mouse.
DR PRO; PR:Q5SQP1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SQP1; protein.
DR Bgee; ENSMUSG00000020419; Expressed in spermatocyte and 25 other tissues.
DR ExpressionAtlas; Q5SQP1; baseline and differential.
DR Genevisible; Q5SQP1; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEP:UniProtKB.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:UniProtKB.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..306
FT /note="HORMA domain-containing protein 2"
FT /id="PRO_0000284670"
FT DOMAIN 29..232
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024605"
FT VAR_SEQ 60..65
FT /note="DRRLDD -> MRRDPN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024606"
SQ SEQUENCE 306 AA; 34812 MW; A0E41A74BA7E3A63 CRC64;
MATAQLSHNT RTLKASKNTI FPSQVTNEHE SLVVVKKLFA TCISCITYLR GLFPESSYRD
RRLDDLSLKI LREDKKCPGS LHIIKWIQGC FDALEKRYLH MAVLTLYTNP KEPEKVTEIY
QFRFKYTKKG TTMDFDSSST SFESGTDSED IKKACSLLIR QLYILMQNLG PLPNDVILTM
KLHYYNSVTP HDYQPPGFKE AVNSHFLLFE GEPVSLRMGS VSSGFHSMKV KVTTEATRML
DGENSVSQDD GTTEIAHQGL DCDEEEEACG SQVQRMNFVH IEPSFESSRK KKKVSEPVTV
FIPNRK
