SHTAP_MOUSE
ID SHTAP_MOUSE Reviewed; 806 AA.
AC C4P6S0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Sperm head and tail associated protein;
GN Name=Nsun4; Synonyms=Shtap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), POTENTIAL FUNCTION,
RP INTERACTION WITH CRISP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=19686095; DOI=10.1042/bc20090099;
RA Jamsai D., Rijal S., Bianco D.M., O'Connor A.E., Merriner D.J., Smith S.J.,
RA Gibbs G.M., O'Bryan M.K.;
RT "A novel protein, sperm head and tail associated protein (SHTAP), interacts
RT with cysteine-rich secretory protein 2 (CRISP2) during spermatogenesis in
RT the mouse.";
RL Biol. Cell 102:93-106(2010).
CC -!- FUNCTION: Plays a role during spermatogenesis. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with CRISP2. {ECO:0000269|PubMed:19686095}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19686095}.
CC Note=Localized to the peri-acrosomal region of the round spermatids as
CC well as the heads and tails of the elongated spermatids and
CC spermatozoa. Redistributed within the head during sperm capacitation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=3;
CC IsoId=C4P6S0-1; Sequence=Displayed;
CC Name=4;
CC IsoId=C4P6S0-2; Sequence=VSP_038426;
CC Name=1;
CC IsoId=Q9CZ57-1; Sequence=External;
CC Name=2;
CC IsoId=Q9CZ57-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoforms 3 and 4 are expressed in testis (at
CC protein level). {ECO:0000269|PubMed:19686095}.
CC -!- DEVELOPMENTAL STAGE: Isoforms 3 and 4 are first detected in testis from
CC postnatal day 18 to adult. {ECO:0000269|PubMed:19686095}.
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DR EMBL; FJ882982; ACQ99317.1; -; mRNA.
DR AlphaFoldDB; C4P6S0; -.
DR STRING; 10090.ENSMUSP00000130430; -.
DR PaxDb; C4P6S0; -.
DR PRIDE; C4P6S0; -.
DR ProteomicsDB; 257228; -. [C4P6S0-1]
DR ProteomicsDB; 257229; -. [C4P6S0-2]
DR Antibodypedia; 32791; 71 antibodies from 19 providers.
DR Ensembl; ENSMUST00000165493; ENSMUSP00000130430; ENSMUSG00000028706. [C4P6S0-1]
DR MGI; MGI:1919431; Nsun4.
DR VEuPathDB; HostDB:ENSMUSG00000028706; -.
DR eggNOG; ENOG502THAH; Eukaryota.
DR GeneTree; ENSGT00500000045816; -.
DR HOGENOM; CLU_018872_0_0_1; -.
DR InParanoid; C4P6S0; -.
DR OMA; DSCEPKP; -.
DR PhylomeDB; C4P6S0; -.
DR ChiTaRS; Nsun4; mouse.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; C4P6S0; protein.
DR Bgee; ENSMUSG00000028706; Expressed in primary oocyte and 269 other tissues.
DR ExpressionAtlas; C4P6S0; baseline and differential.
DR Genevisible; C4P6S0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; ISO:MGI.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR InterPro; IPR023267; RCMT.
DR PANTHER; PTHR22808; PTHR22808; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Reference proteome.
FT CHAIN 1..806
FT /note="Sperm head and tail associated protein"
FT /id="PRO_0000389442"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..806
FT /note="Interaction with CRISP2"
FT /evidence="ECO:0000269|PubMed:19686095"
FT REGION 707..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..295
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19686095"
FT /id="VSP_038426"
SQ SEQUENCE 806 AA; 86304 MW; 770DB477A0BD7B19 CRC64;
MNSSPPFLLK ISAPSTSPQA DCPNNYSFPP ESPSSCRKGF TPVLTLEVPV APGKDFNDHL
SCNAGLSPNA GNRFTNPPYS REPFSCLTIS SPCLPRRIPT PPPPPPVLSS PPPPERCPFE
PFSPLLGRLY RQEPAGSSSP CFDRFSLQGS PSPHQRNLCC NYIDSPESQR SCPPSPRLCY
VTSPPLIHQA PRASPVTSPE LTHITLETGP VISTPLMPGS QGNYSIISPL LTHRPLRPGL
AISPPLAHRS VETRPLTPAS ISHRGPHCPS RRSYNDPPLS SASSPPSGNP YHDNPMPPNS
CEPKPQLDVP LGKNGCGPPL SSQAGMSGSP ISPQEGCIHY SHLCPDSQIS APRSPFCVIN
LPPESAGSPS SSLPQALQKP CVGSFLWEPG GNSYLLLTPG TIISGPSCTT GPPLPQCPNP
SPYFPSPLNN QCVAPPQSPR GYNEPRPPTS APPQMKSPKS PESRRNPYKC RSLDNTPHHT
PPSHSKSHKT NTCPQPPSQS FGLFSPCMEP AITTTSNSCP KEPPPETAVL KTVAPTSCPH
SSPCNPALPS RYPKSSPHVP PPVSPCNTHM YSVVPPTSHL SPLSSPLNQS IPLPQPAVLP
CGTYSAPRGP PSHIKSVAPP CSTHIYSFIP LRTPFDPRCL PVVPRARFCP TTVPCGIHTY
AVTSPVPLNN PSQIPYSCSL PPSKTSSTCS TSVSSTIVCS DYQSSDSQIN HQNKSQSPNK
NSSLHNQSKS PLRRGAFQSR SRSRSSSPLQ SSTQDRNEST NMGVKHHKRS RKQSQSPADG
KIESQSKSLQ HRKSVGQIKS PHSKKK