HORM1_MOUSE
ID HORM1_MOUSE Reviewed; 392 AA.
AC Q9D5T7; Q9CUF3; Q9D473;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=HORMA domain-containing protein 1 {ECO:0000312|MGI:MGI:1915231};
DE AltName: Full=Newborn ovary HORMA protein {ECO:0000303|PubMed:15567723};
GN Name=Hormad1 {ECO:0000312|MGI:MGI:1915231};
GN Synonyms=Nohma {ECO:0000303|PubMed:15567723};
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/SvEv; TISSUE=Ovary;
RX PubMed=15567723; DOI=10.1016/j.modgep.2004.07.008;
RA Pangas S.A., Yan W., Matzuk M.M., Rajkovic A.;
RT "Restricted germ cell expression of a gene encoding a novel mammalian HORMA
RT domain-containing protein.";
RL Gene Expr. Patterns 5:257-263(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 IDENTIFICATION (ISOFORM 2).
RX PubMed=15999985;
RA Chen Y.-T., Venditti C.A., Theiler G., Stevenson B.J., Iseli C., Gure A.O.,
RA Jongeneel C.V., Old L.J., Simpson A.J.G.;
RT "Identification of CT46/HORMAD1, an immunogenic cancer/testis antigen
RT encoding a putative meiosis-related protein.";
RL Cancer Immun. 5:9-9(2005).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, 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 [7]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19686734; DOI=10.1016/j.yexcr.2009.08.007;
RA Fukuda T., Daniel K., Wojtasz L., Toth A., Hoog C.;
RT "A novel mammalian HORMA domain-containing protein, HORMAD1, preferentially
RT associates with unsynapsed meiotic chromosomes.";
RL Exp. Cell Res. 316:158-171(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21079677; DOI=10.1371/journal.pgen.1001190;
RA Shin Y.H., Choi Y., Erdin S.U., Yatsenko S.A., Kloc M., Yang F., Wang P.J.,
RA Meistrich M.L., Rajkovic A.;
RT "Hormad1 mutation disrupts synaptonemal complex formation, recombination,
RT and chromosome segregation in mammalian meiosis.";
RL PLoS Genet. 6:E1001190-E1001190(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21478856; DOI=10.1038/ncb2213;
RA Daniel K., Lange J., Hached K., Fu J., Anastassiadis K., Roig I.,
RA Cooke H.J., Stewart A.F., Wassmann K., Jasin M., Keeney S., Toth A.;
RT "Meiotic homologue alignment and its quality surveillance are controlled by
RT mouse HORMAD1.";
RL Nat. Cell Biol. 13:599-610(2011).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HORMAD2.
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 [11]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-375.
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).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IHO1.
RX PubMed=27723721; DOI=10.1038/ncb3417;
RA Stanzione M., Baumann M., Papanikos F., Dereli I., Lange J., Ramlal A.,
RA Traenkner D., Shibuya H., de Massy B., Watanabe Y., Jasin M., Keeney S.,
RA Toth A.;
RT "Meiotic DNA break formation requires the unsynapsed chromosome axis-
RT binding protein IHO1 (CCDC36) in mice.";
RL Nat. Cell Biol. 18:1208-1220(2016).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
CC -!- FUNCTION: Plays a key role in meiotic progression (PubMed:19686734,
CC PubMed:21079677, PubMed:21478856). Regulates 3 different functions
CC during meiosis: ensures that sufficient numbers of processed DNA
CC double-strand breaks (DSBs) are available for successful homology
CC search by increasing the steady-state numbers of single-stranded DSB
CC ends (PubMed:19686734, PubMed:21079677). Promotes synaptonemal-complex
CC formation independently of its role in homology search
CC (PubMed:19686734, PubMed:21079677). 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 (PubMed:21478856). {ECO:0000269|PubMed:19686734,
CC ECO:0000269|PubMed:21079677, ECO:0000269|PubMed:21478856}.
CC -!- SUBUNIT: Interacts with HORMAD2 (PubMed:22549958). Interacts with IHO1
CC (PubMed:27723721). {ECO:0000269|PubMed:22549958,
CC ECO:0000269|PubMed:27723721}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446}. Chromosome
CC {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446,
CC ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:22549958,
CC ECO:0000269|PubMed:27723721, ECO:0000269|PubMed:30272023,
CC ECO:0000269|PubMed:30746471}. Note=Preferentially localizes to
CC unsynapsed or desynapsed chromosomal regions during the prophase I
CC stage of meiosis (PubMed:19851446, PubMed:19686734, PubMed:27723721).
CC Accumulates on the chromosomes during the leptotene to zygotene stages
CC of meiotic prophase I (PubMed:19851446, PubMed:19686734,
CC PubMed:27723721). As germ cells progress into the pachytene stage,
CC disappears from the synapsed chromosomal regions (PubMed:19851446,
CC PubMed:19686734, PubMed:27723721). Once the chromosomes desynapse
CC during the diplotene stage, it again accumulates on the chromosome axis
CC of the desynapsed homologs (PubMed:19851446, PubMed:19686734,
CC PubMed:27723721). TRIP13 is required for depletion from synapsed
CC chromosomes (PubMed:19851446). The expression of the phosphorylated
CC form at Ser-375 is restricted to unsynapsed chromosomal regions
CC (PubMed:22346761). {ECO:0000269|PubMed:19686734,
CC ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761,
CC ECO:0000269|PubMed:27723721}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:19686734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=HORMAD1L;
CC IsoId=Q9D5T7-1; Sequence=Displayed;
CC Name=2; Synonyms=HORMAD1S;
CC IsoId=Q9D5T7-2; Sequence=VSP_024604;
CC -!- TISSUE SPECIFICITY: Specifically expressed in meiotic germ cells.
CC {ECO:0000269|PubMed:15567723, ECO:0000269|PubMed:19686734,
CC ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:21079677}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spermatocytes from P10 to adulthood.
CC Expressed in oocytes from 12.5 dpc to P9. Primarily detected in
CC spermatocytes and less in spermatids or spermatogonia. Abundant in the
CC nuclei of pachytene and zygotene cells. Also detected in nuclei of
CC diplotene cells (at protein level). {ECO:0000269|PubMed:15567723,
CC ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:21079677}.
CC -!- PTM: Phosphorylated at Ser-375 in a SPO11-dependent manner.
CC {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:22346761}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally without obvious somatic
CC defects but males and females are sterile. Although spermatocytes are
CC present in testis tubules at epithelial cycle stage III-IV, they
CC undergo apoptosis by the end of stage IV, and post-meiotic cells are
CC not found in testes, suggesting that spermatocytes are eliminated at a
CC stage equivalent to mid-pachytene. In females, ovarian development is
CC grossly normal, eggs fertilize and embryonic development arrests at
CC blastocyst stage due to aneuploidy. {ECO:0000269|PubMed:21079677,
CC ECO:0000269|PubMed:21478856}.
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DR EMBL; AY626343; AAT45739.1; -; mRNA.
DR EMBL; AY634284; AAT47126.1; -; mRNA.
DR EMBL; AK014945; BAB29633.1; -; mRNA.
DR EMBL; AK016324; BAB30195.1; -; mRNA.
DR EMBL; AK016743; BAB30406.1; -; mRNA.
DR EMBL; AK163995; BAE37577.1; -; mRNA.
DR EMBL; BC051129; AAH51129.1; -; mRNA.
DR CCDS; CCDS38547.1; -. [Q9D5T7-2]
DR CCDS; CCDS71292.1; -. [Q9D5T7-1]
DR RefSeq; NP_001276461.1; NM_001289532.1. [Q9D5T7-1]
DR RefSeq; NP_001276463.1; NM_001289534.1. [Q9D5T7-2]
DR RefSeq; NP_001276466.1; NM_001289537.1. [Q9D5T7-2]
DR RefSeq; NP_080765.1; NM_026489.3. [Q9D5T7-2]
DR AlphaFoldDB; Q9D5T7; -.
DR SMR; Q9D5T7; -.
DR BioGRID; 212580; 1.
DR IntAct; Q9D5T7; 1.
DR STRING; 10090.ENSMUSP00000029754; -.
DR iPTMnet; Q9D5T7; -.
DR PhosphoSitePlus; Q9D5T7; -.
DR PaxDb; Q9D5T7; -.
DR PRIDE; Q9D5T7; -.
DR ProteomicsDB; 273163; -. [Q9D5T7-1]
DR ProteomicsDB; 273164; -. [Q9D5T7-2]
DR Antibodypedia; 34037; 204 antibodies from 25 providers.
DR Ensembl; ENSMUST00000029754; ENSMUSP00000029754; ENSMUSG00000028109. [Q9D5T7-1]
DR Ensembl; ENSMUST00000090797; ENSMUSP00000088303; ENSMUSG00000028109. [Q9D5T7-2]
DR Ensembl; ENSMUST00000107154; ENSMUSP00000102772; ENSMUSG00000028109. [Q9D5T7-2]
DR Ensembl; ENSMUST00000171191; ENSMUSP00000127180; ENSMUSG00000028109. [Q9D5T7-2]
DR GeneID; 67981; -.
DR KEGG; mmu:67981; -.
DR UCSC; uc008qkb.2; mouse. [Q9D5T7-2]
DR UCSC; uc008qkd.2; mouse. [Q9D5T7-1]
DR CTD; 84072; -.
DR MGI; MGI:1915231; Hormad1.
DR VEuPathDB; HostDB:ENSMUSG00000028109; -.
DR eggNOG; KOG4652; Eukaryota.
DR GeneTree; ENSGT00390000018130; -.
DR HOGENOM; CLU_058638_1_0_1; -.
DR InParanoid; Q9D5T7; -.
DR OMA; GNCEGVI; -.
DR OrthoDB; 1038689at2759; -.
DR PhylomeDB; Q9D5T7; -.
DR TreeFam; TF313989; -.
DR BioGRID-ORCS; 67981; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Hormad1; mouse.
DR PRO; PR:Q9D5T7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D5T7; protein.
DR Bgee; ENSMUSG00000028109; Expressed in spermatocyte and 15 other tissues.
DR Genevisible; Q9D5T7; MM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEP:UniProtKB.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:UniProtKB.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0060629; P:regulation of homologous chromosome segregation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; 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; Cytoplasm; Differentiation; Meiosis;
KW Nucleus; Oogenesis; Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..392
FT /note="HORMA domain-containing protein 1"
FT /id="PRO_0000284666"
FT DOMAIN 25..227
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT REGION 323..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 381..384
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 332..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22346761,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 368..392
FT /note="VLHVLESSQESVLKKRRVSEPKEHT -> INAPECR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15567723, ECO:0000303|PubMed:16141072"
FT /id="VSP_024604"
FT CONFLICT 140
FT /note="S -> Y (in Ref. 2; BAB30195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 44933 MW; 891D1A76CFE242F1 CRC64;
MATMQLQRTA SLSALVFPNK ISTEHQSLMF VKRLLAVSVS CITYLRGIFP ERAYGTRYLD
DLCVKILKED KNCPGSSQLV KWMLGCYDAL QKKYLRMIIL AVYTNPGDPQ TISECYQFKF
KYTKNGPIMD FISKNQNNKS STTSADTKKA SILLIRKIYV LMQNLGPLPN DVCLTMKLFY
YDEVTPPDYQ PPGFKDGDCE GVIFDGDPTY LNVGEVPTPF HTFRLKVTTE KERMENIDST
ILKPKESKTQ FEKILMDKDD VEDENHNNFD IKTKMNEQNE NSGASEIKEP NLDCKEEETM
QFKKSQSPSI SHCQVEQLVS KTSELDVSES KTRSGKIFQS KMVNGNNQQG QTSKENRKRS
LRQFRKTVLH VLESSQESVL KKRRVSEPKE HT
