ID   HORM1_PIG               Reviewed;         394 AA.
AC   E2IUK4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=HORMA domain-containing protein 1;
GN   Name=HORMAD1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu Y.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a key role in meiotic progression. Regulates 3
CC       different functions during meiosis: ensures that sufficient numbers of
CC       processed DNA double-strand breaks (DSBs) are available for successful
CC       homology search by increasing the steady-state numbers of single-
CC       stranded DSB ends. Promotes synaptonemal-complex formation
CC       independently of its role in homology search. Plays a key role in the
CC       male mid-pachytene checkpoint and the female meiotic prophase
CC       checkpoint: required for efficient build-up of ATR activity on
CC       unsynapsed chromosome regions, a process believed to form the basis of
CC       meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase
CC       quality control in both sexes. {ECO:0000250|UniProtKB:Q9D5T7}.
CC   -!- SUBUNIT: Interacts with HORMAD2. Interacts with IHO1.
CC       {ECO:0000250|UniProtKB:Q9D5T7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D5T7}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9D5T7}. Note=Preferentially
CC       localizes to unsynapsed or desynapsed chromosomal regions during the
CC       prophase I stage of meiosis. TRIP13 is required for depletion from
CC       synapsed chromosomes. The expression of the phosphorylated form at Ser-
CC       377 is restricted to unsynapsed chromosomal regions (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D5T7}.
CC   -!- PTM: Phosphorylated at Ser-377 in a SPO11-dependent manner.
CC       {ECO:0000250|UniProtKB:Q9D5T7}.
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DR   EMBL; HM627267; ADK36685.1; -; mRNA.
DR   RefSeq; NP_001181910.1; NM_001194981.1.
DR   AlphaFoldDB; E2IUK4; -.
DR   SMR; E2IUK4; -.
DR   STRING; 9823.ENSSSCP00000007090; -.
DR   PaxDb; E2IUK4; -.
DR   PRIDE; E2IUK4; -.
DR   GeneID; 100499502; -.
DR   KEGG; ssc:100499502; -.
DR   CTD; 84072; -.
DR   eggNOG; KOG4652; Eukaryota.
DR   InParanoid; E2IUK4; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; ISS:UniProtKB.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0051177; P:meiotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR   GO; GO:0060629; P:regulation of homologous chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0007130; P:synaptonemal complex assembly; ISS: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   2: Evidence at transcript level;
KW   Chromosome; Differentiation; Meiosis; Nucleus; Oogenesis; Phosphoprotein;
KW   Reference proteome; Spermatogenesis.
FT   CHAIN           1..394
FT                   /note="HORMA domain-containing protein 1"
FT                   /id="PRO_0000410913"
FT   DOMAIN          24..226
FT                   /note="HORMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT   REGION          306..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           383..386
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        309..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5T7"
SQ   SEQUENCE   394 AA;  44980 MW;  38CED56CA64B9A23 CRC64;
     MATAQLQRTS MSALVFPNKI STEQQSLVLV KRLLAVSVSC ITYLRGIFPE CAYGTRYLDD
     LCVKILREDK NCPGSTQLVK WMLGCYDALQ KKYLRMVVLA VYTNPEDPQT ISECYQFKFK
     YTSNGPIMDF ISKNQSSESS MSSADTKKAS ILLIRKIYIL MQNLGPLPND VCLTMKLFYY
     DEVTPPDYQP PGFKDGDCEG VIFEGEPMYL NVGEVPTPFH TFKVKVTTEK ERMENIYSGI
     LSPKQIKTPL QKILMDKDDL EDEQEHYIND DFDIETKMEE QKKKLGSSEL GEPNLVCEED
     EIMRSKESPE LSISHSQVEQ LVSKTSELDV SESKTRSGKI FQNKMANGNQ QIKSKESRKR
     SQLESGKTVL HHFDSSSQDS VPKRRKFSEP KEHI