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HORM1_MACFA
ID   HORM1_MACFA             Reviewed;         394 AA.
AC   Q4R8B9; Q95JJ3; Q95JZ3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=HORMA domain-containing protein 1;
GN   Name=HORMAD1; ORFNames=QtsA-11904, QtsA-12863, QtsA-16861;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-394.
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-394.
RC   TISSUE=Testis;
RA   Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA   Sugano S.;
RT   "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT   libraries.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION.
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB62979.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB63133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB168538; BAE00653.1; -; mRNA.
DR   EMBL; AB070034; BAB62979.1; ALT_INIT; mRNA.
DR   EMBL; AB070188; BAB63133.1; ALT_INIT; mRNA.
DR   RefSeq; XP_005542028.1; XM_005541971.2.
DR   RefSeq; XP_005542029.1; XM_005541972.2.
DR   AlphaFoldDB; Q4R8B9; -.
DR   SMR; Q4R8B9; -.
DR   STRING; 9541.XP_005542028.1; -.
DR   PRIDE; Q4R8B9; -.
DR   Ensembl; ENSMFAT00000020530; ENSMFAP00000009464; ENSMFAG00000000795.
DR   GeneID; 101867396; -.
DR   KEGG; mcf:101867396; -.
DR   CTD; 84072; -.
DR   VEuPathDB; HostDB:ENSMFAG00000000795; -.
DR   eggNOG; KOG4652; Eukaryota.
DR   GeneTree; ENSGT00390000018130; -.
DR   OMA; GNCEGVI; -.
DR   OrthoDB; 1038689at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000000795; Expressed in multicellular organism.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
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_0000284665"
FT   DOMAIN          24..226
FT                   /note="HORMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT   REGION          252..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           383..386
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        252..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..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"
FT   CONFLICT        283
FT                   /note="N -> D (in Ref. 3; BAB62979)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  45163 MW;  18B40DB3C68FBA22 CRC64;
     MATAQLQRTP MSALVFPNKI STEHQSLVLV KRLLAVSVSC ITYLRGIFPE CAYGTRYLDD
     LCVKILREDK NCPGSTQLVK WMLGCYDALQ KKYLRMVVLA VYTNPEDPQT ISECYQFKFK
     YTNNGPLMDF ISKNQSNESS MSSTDTKKAS ILLIRKIYIL MQNLGPLPND VCLTMKLFYY
     DEVTPPDYQP PGFKDGDCEG VIFEGEPMYL NVGEVSTPFH IFKVKVTTER ERMENIDSTI
     LSPKQIKTPF QKILRDKDVE DEQEHYTSDD LDMETKMEEQ EKNPASSELG EPSLVCEEDE
     IMRSKESPDL SISHSQVEQL VNKTSELDMS ESKTRSGKVF QNKMANGNQP VKSSKENRKR
     SQHESGRRVL HHFDSSSQES VPKRRKFSEP KEHI
 
 
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