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HORM1_RAT
ID   HORM1_RAT               Reviewed;         392 AA.
AC   D3ZWE7; D3ZZR2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=HORMA domain-containing protein 1;
GN   Name=Hormad1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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       375 is restricted to unsynapsed chromosomal regions (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D5T7}.
CC   -!- PTM: Phosphorylated at Ser-375 in a SPO11-dependent manner.
CC       {ECO:0000250|UniProtKB:Q9D5T7}.
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DR   EMBL; CH474015; EDL85702.1; -; Genomic_DNA.
DR   RefSeq; NP_001102419.1; NM_001108949.1.
DR   RefSeq; XP_006233013.1; XM_006232951.3.
DR   AlphaFoldDB; D3ZWE7; -.
DR   SMR; D3ZWE7; -.
DR   STRING; 10116.ENSRNOP00000063863; -.
DR   CarbonylDB; D3ZWE7; -.
DR   iPTMnet; D3ZWE7; -.
DR   PhosphoSitePlus; D3ZWE7; -.
DR   PaxDb; D3ZWE7; -.
DR   PRIDE; D3ZWE7; -.
DR   Ensembl; ENSRNOT00000066821; ENSRNOP00000063863; ENSRNOG00000021160.
DR   GeneID; 365868; -.
DR   KEGG; rno:365868; -.
DR   CTD; 84072; -.
DR   RGD; 1564960; Hormad1.
DR   eggNOG; KOG4652; Eukaryota.
DR   GeneTree; ENSGT00390000018130; -.
DR   HOGENOM; CLU_058638_1_0_1; -.
DR   InParanoid; D3ZWE7; -.
DR   OMA; GNCEGVI; -.
DR   OrthoDB; 1038689at2759; -.
DR   TreeFam; TF313989; -.
DR   PRO; PR:D3ZWE7; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Proteomes; UP000234681; Chromosome 2.
DR   Bgee; ENSRNOG00000021160; Expressed in testis and 3 other tissues.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000795; C:synaptonemal complex; ISO:RGD.
DR   GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
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   1: Evidence at protein level;
KW   Chromosome; Differentiation; Meiosis; Nucleus; Oogenesis; Phosphoprotein;
KW   Reference proteome; Spermatogenesis.
FT   CHAIN           1..392
FT                   /note="HORMA domain-containing protein 1"
FT                   /id="PRO_0000410914"
FT   DOMAIN          25..227
FT                   /note="HORMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT   REGION          271..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           381..384
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        274..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5T7"
SQ   SEQUENCE   392 AA;  44885 MW;  9988EC445088A9F3 CRC64;
     MATMQLRRTA SMSALVFPNK ISTEQQSLMF VKRLLAVSVS CITYLRGIFP ERAYGTRYLD
     DLCVKILKED KNCPGSSQLV KWMLGCYDAL QKKYLRMIIL AVYTNPEDPQ TISECYQFKF
     KYTKNGPIMD FISKNQNNKS STTSADTKKA SILLIRKIYV LMQNLGPLPN DVCLTMKLFY
     YDEVTPPDYQ PPGFKDGDCE GVIFDGDPTY LNVGEVPTPF HTFRLKVTTE KERMENIDSA
     ILTPKDSKIP FQKILMDKDD VEDENHNNFD IKTKMNEQNE NSGTSEIKEP NLDCKEEEIM
     QFKKNQSSSI SQCQVEQLIS KTSELDVSES KTRSGKIFQC KMVNGNQQGQ ISKENRKRSL
     RQSGKTVLHI LESSSQESVL KRRRVSEPNE HT
 
 
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