HORM1_CANLF
ID HORM1_CANLF Reviewed; 395 AA.
AC E2RSQ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=HORMA domain-containing protein 1;
GN Name=HORMAD1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
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 378 is restricted to unsynapsed chromosomal regions (By similarity).
CC {ECO:0000250|UniProtKB:Q9D5T7}.
CC -!- PTM: Phosphorylated at Ser-378 in a SPO11-dependent manner.
CC {ECO:0000250|UniProtKB:Q9D5T7}.
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DR AlphaFoldDB; E2RSQ2; -.
DR SMR; E2RSQ2; -.
DR STRING; 9612.ENSCAFP00000017772; -.
DR PaxDb; E2RSQ2; -.
DR eggNOG; KOG4652; Eukaryota.
DR InParanoid; E2RSQ2; -.
DR Proteomes; UP000002254; 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 3: Inferred from homology;
KW Chromosome; Differentiation; Meiosis; Nucleus; Oogenesis; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..395
FT /note="HORMA domain-containing protein 1"
FT /id="PRO_0000410912"
FT DOMAIN 24..226
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT REGION 329..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 384..387
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D5T7"
SQ SEQUENCE 395 AA; 44926 MW; B898E8FC3E26AB2F CRC64;
MATAQLQRTS MSALVFPNKI STEQQSLVLV KRLLAVSVSC ITYLRGIFPE CAYGTRYLDD
LCVKILREDK NCPGSTQLVK WMLGCYDALQ KKYLRMVVLA VYTNPEDPQT ISECYQFKFK
YASNGPVMDF ISKNQSSESS MSSADTKKAS ILLIRKIYIL MQNLGPLPND VCLTMKLFYY
DEVTPPDYQP PGFKDGDCEG VIFEGEPMYL NVGEVPTPFH TFKVKVTTEK ERMENIDSAI
LSPKQLKTPL QKILMDKDDV ADEQEHYISD DFDVETKMEE QKRNLGSSEL GEPSLVCEED
EIMRSKESLD LSISHSQVEQ LVSKTSELDV SESKTRSGKI FQNKMANGNQ PVKSSKENRK
RNQLESGKTV LYHFDSSSQE SVPKRRKFSE PKEYV
