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HORMA domain-containing protein 1 (Newborn ovary HORMA protein)

 HORM1_MOUSE             Reviewed;         392 AA.
Q9D5T7; Q9CUF3; Q9D473;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
07-JUN-2017, entry version 99.
RecName: Full=HORMA domain-containing protein 1 {ECO:0000312|MGI:MGI:1915231};
AltName: Full=Newborn ovary HORMA protein {ECO:0000303|PubMed:15567723};
Name=Hormad1 {ECO:0000312|MGI:MGI:1915231};
Synonyms=Nohma {ECO:0000303|PubMed:15567723};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=129/SvEv; TISSUE=Ovary;
PubMed=15567723; DOI=10.1016/j.modgep.2004.07.008;
Pangas S.A., Yan W., Matzuk M.M., Rajkovic A.;
"Restricted germ cell expression of a gene encoding a novel mammalian
HORMA domain-containing protein.";
Gene Expr. Patterns 5:257-263(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION (ISOFORM 2).
PubMed=15999985;
Chen Y.-T., Venditti C.A., Theiler G., Stevenson B.J., Iseli C.,
Gure A.O., Jongeneel C.V., Old L.J., Simpson A.J.G.;
"Identification of CT46/HORMAD1, an immunogenic cancer/testis antigen
encoding a putative meiosis-related protein.";
Cancer Immun. 5:9-9(2005).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19851446; DOI=10.1371/journal.pgen.1000702;
Wojtasz L., Daniel K., Roig I., Bolcun-Filas E., Xu H., Boonsanay V.,
Eckmann C.R., Cooke H.J., Jasin M., Keeney S., McKay M.J., Toth A.;
"Mouse HORMAD1 and HORMAD2, two conserved meiotic chromosomal
proteins, are depleted from synapsed chromosome axes with the help of
TRIP13 AAA-ATPase.";
PLoS Genet. 5:E1000702-E1000702(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, PHOSPHORYLATION, AND DEVELOPMENTAL STAGE.
PubMed=19686734; DOI=10.1016/j.yexcr.2009.08.007;
Fukuda T., Daniel K., Wojtasz L., Toth A., Hoog C.;
"A novel mammalian HORMA domain-containing protein, HORMAD1,
preferentially associates with unsynapsed meiotic chromosomes.";
Exp. Cell Res. 316:158-171(2010).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=21079677; DOI=10.1371/journal.pgen.1001190;
Shin Y.H., Choi Y., Erdin S.U., Yatsenko S.A., Kloc M., Yang F.,
Wang P.J., Meistrich M.L., Rajkovic A.;
"Hormad1 mutation disrupts synaptonemal complex formation,
recombination, and chromosome segregation in mammalian meiosis.";
PLoS Genet. 6:E1001190-E1001190(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21478856; DOI=10.1038/ncb2213;
Daniel K., Lange J., Hached K., Fu J., Anastassiadis K., Roig I.,
Cooke H.J., Stewart A.F., Wassmann K., Jasin M., Keeney S., Toth A.;
"Meiotic homologue alignment and its quality surveillance are
controlled by mouse HORMAD1.";
Nat. Cell Biol. 13:599-610(2011).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH HORMAD2.
PubMed=22549958; DOI=10.1101/gad.187559.112;
Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J.,
Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.;
"Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
monitored by distinct HORMAD2-independent and -dependent mechanisms.";
Genes Dev. 26:958-973(2012).
[11]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-375.
PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
Fukuda T., Pratto F., Schimenti J.C., Turner J.M.,
Camerini-Otero R.D., Hoeoeg C.;
"Phosphorylation of chromosome core components may serve as axis marks
for the status of chromosomal events during mammalian meiosis.";
PLoS Genet. 8:E1002485-E1002485(2012).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH CCDC36.
PubMed=27723721; DOI=10.1038/ncb3417;
Stanzione M., Baumann M., Papanikos F., Dereli I., Lange J.,
Ramlal A., Traenkner D., Shibuya H., de Massy B., Watanabe Y.,
Jasin M., Keeney S., Toth A.;
"Meiotic DNA break formation requires the unsynapsed chromosome axis-
binding protein IHO1 (CCDC36) in mice.";
Nat. Cell Biol. 18:1208-1220(2016).
-!- FUNCTION: Plays a key role in meiotic progression
(PubMed:19686734, PubMed:21079677, PubMed:21478856). Regulates 3
different functions during meiosis: ensures that sufficient
numbers of processed DNA double-strand breaks (DSBs) are available
for successful homology search by increasing the steady-state
numbers of single-stranded DSB ends (PubMed:19686734,
PubMed:21079677). Promotes synaptonemal-complex formation
independently of its role in homology search (PubMed:19686734,
PubMed:21079677). Plays a key role in the male mid-pachytene
checkpoint and the female meiotic prophase checkpoint: required
for efficient build-up of ATR activity on unsynapsed chromosome
regions, a process believed to form the basis of meiotic silencing
of unsynapsed chromatin (MSUC) and meiotic prophase quality
control in both sexes (PubMed:21478856).
{ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:21079677,
ECO:0000269|PubMed:21478856}.
-!- SUBUNIT: Interacts with HORMAD2 (PubMed:22549958). Interacts with
IHO1/CCDC36 (PubMed:27723721). {ECO:0000269|PubMed:22549958,
ECO:0000269|PubMed:27723721}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446}.
Chromosome {ECO:0000269|PubMed:19686734,
ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761,
ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:27723721}.
Note=Preferentially localizes to unsynapsed or desynapsed
chromosomal regions during the prophase I stage of meiosis
(PubMed:19851446, PubMed:19686734, PubMed:27723721). Accumulates
on the chromosomes during the leptotene to zygotene stages of
meiotic prophase I (PubMed:19851446, PubMed:19686734,
PubMed:27723721). As germ cells progress into the pachytene stage,
disappears from the synapsed chromosomal regions (PubMed:19851446,
PubMed:19686734, PubMed:27723721). Once the chromosomes desynapse
during the diplotene stage, it again accumulates on the chromosome
axis of the desynapsed homologs (PubMed:19851446, PubMed:19686734,
PubMed:27723721). TRIP13 is required for depletion from synapsed
chromosomes (PubMed:19851446). The expression of the
phosphorylated form at Ser-375 is restricted to unsynapsed
chromosomal regions (PubMed:22346761).
{ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446,
ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:27723721}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:19686734}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=HORMAD1L;
IsoId=Q9D5T7-1; Sequence=Displayed;
Name=2; Synonyms=HORMAD1S;
IsoId=Q9D5T7-2; Sequence=VSP_024604;
-!- TISSUE SPECIFICITY: Specifically expressed in meiotic germ cells.
{ECO:0000269|PubMed:15567723, ECO:0000269|PubMed:19686734,
ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:21079677}.
-!- DEVELOPMENTAL STAGE: Expressed in spermatocytes from P10 to
adulthood. Expressed in oocytes from E12.5 to P9. Primarily
detected in spermatocytes and less in spermatids or spermatogonia.
Abundant in the nuclei of pachytene and zygotene cells. Also
detected in nuclei of diplotene cells (at protein level).
{ECO:0000269|PubMed:15567723, ECO:0000269|PubMed:19686734,
ECO:0000269|PubMed:21079677}.
-!- PTM: Phosphorylated at Ser-375 in a SPO11-dependent manner.
{ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:22346761}.
-!- DISRUPTION PHENOTYPE: Mice develop normally without obvious
somatic defects but males and females are sterile. Although
spermatocytes are present in testis tubules at epithelial cycle
stage III-IV, they undergo apoptosis by the end of stage IV, and
post-meiotic cells are not found in testes, suggesting that
spermatocytes are eliminated at a stage equivalent to mid-
pachytene. In females, ovarian development is grossly normal, eggs
fertilize and embryonic development arrests at blastocyst stage
due to aneuploidy. {ECO:0000269|PubMed:21079677,
ECO:0000269|PubMed:21478856}.
-----------------------------------------------------------------------
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EMBL; AY626343; AAT45739.1; -; mRNA.
EMBL; AY634284; AAT47126.1; -; mRNA.
EMBL; AK014945; BAB29633.1; -; mRNA.
EMBL; AK016324; BAB30195.1; -; mRNA.
EMBL; AK016743; BAB30406.1; -; mRNA.
EMBL; AK163995; BAE37577.1; -; mRNA.
EMBL; BC051129; AAH51129.1; -; mRNA.
CCDS; CCDS38547.1; -. [Q9D5T7-2]
CCDS; CCDS71292.1; -. [Q9D5T7-1]
RefSeq; NP_001276461.1; NM_001289532.1. [Q9D5T7-1]
RefSeq; NP_001276463.1; NM_001289534.1. [Q9D5T7-2]
RefSeq; NP_001276466.1; NM_001289537.1. [Q9D5T7-2]
RefSeq; NP_080765.1; NM_026489.3. [Q9D5T7-2]
UniGene; Mm.179050; -.
ProteinModelPortal; Q9D5T7; -.
SMR; Q9D5T7; -.
BioGrid; 212580; 1.
IntAct; Q9D5T7; 1.
STRING; 10090.ENSMUSP00000088303; -.
iPTMnet; Q9D5T7; -.
PhosphoSitePlus; Q9D5T7; -.
PaxDb; Q9D5T7; -.
PRIDE; Q9D5T7; -.
Ensembl; ENSMUST00000029754; ENSMUSP00000029754; ENSMUSG00000028109. [Q9D5T7-1]
Ensembl; ENSMUST00000090797; ENSMUSP00000088303; ENSMUSG00000028109. [Q9D5T7-2]
Ensembl; ENSMUST00000107154; ENSMUSP00000102772; ENSMUSG00000028109. [Q9D5T7-2]
Ensembl; ENSMUST00000171191; ENSMUSP00000127180; ENSMUSG00000028109. [Q9D5T7-2]
GeneID; 67981; -.
KEGG; mmu:67981; -.
UCSC; uc008qkb.2; mouse. [Q9D5T7-2]
UCSC; uc008qkd.2; mouse. [Q9D5T7-1]
CTD; 84072; -.
MGI; MGI:1915231; Hormad1.
eggNOG; KOG4652; Eukaryota.
eggNOG; ENOG410XT4N; LUCA.
GeneTree; ENSGT00390000018130; -.
HOGENOM; HOG000293366; -.
HOVERGEN; HBG074209; -.
InParanoid; Q9D5T7; -.
OMA; KYLRMVV; -.
OrthoDB; EOG091G0F8O; -.
TreeFam; TF313989; -.
PRO; PR:Q9D5T7; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028109; -.
CleanEx; MM_HORMAD1; -.
Genevisible; Q9D5T7; MM.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
GO; GO:0001824; P:blastocyst development; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEP:UniProtKB.
GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:UniProtKB.
GO; GO:0051598; P:meiotic recombination checkpoint; IMP:UniProtKB.
GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:UniProtKB.
GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
GO; GO:0060629; P:regulation of homologous chromosome segregation; IMP:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0007129; P:synapsis; IMP:MGI.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
InterPro; IPR003511; HORMA_dom.
Pfam; PF02301; HORMA; 1.
SUPFAM; SSF56019; SSF56019; 1.
PROSITE; PS50815; HORMA; 1.
1: Evidence at protein level;
Alternative splicing; Chromosome; Complete proteome; Cytoplasm;
Differentiation; Meiosis; Nucleus; Oogenesis; Phosphoprotein;
Reference proteome; Spermatogenesis.
CHAIN 1 392 HORMA domain-containing protein 1.
/FTId=PRO_0000284666.
DOMAIN 25 227 HORMA. {ECO:0000255|PROSITE-
ProRule:PRU00109}.
MOTIF 381 384 Nuclear localization signal.
{ECO:0000305}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:22346761}.
VAR_SEQ 368 392 VLHVLESSQESVLKKRRVSEPKEHT -> INAPECR (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15567723,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024604.
CONFLICT 140 140 S -> Y (in Ref. 2; BAB30195).
{ECO:0000305}.
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


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