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ZPBP1_MOUSE
ID   ZPBP1_MOUSE             Reviewed;         350 AA.
AC   Q62522; Q9CR97;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Zona pellucida-binding protein 1;
DE   AltName: Full=Inner acrosomal membrane IAM38 {ECO:0000303|PubMed:19204925};
DE   AltName: Full=Sp38;
DE   Flags: Precursor;
GN   Name=Zpbp; Synonyms=Zpbp1;
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].
RC   STRAIN=ddY; TISSUE=Testis;
RA   Baba T., Mori E., Mori T., Kashiwabara S., Tanaka K.;
RT   "Expression of the gene encoding zona-pellucida-binding protein, sp38,
RT   during spermatogenesis.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-350.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17664285; DOI=10.1128/mcb.01029-07;
RA   Lin Y.N., Roy A., Yan W., Burns K.H., Matzuk M.M.;
RT   "Loss of zona pellucida binding proteins in the acrosomal matrix disrupts
RT   acrosome biogenesis and sperm morphogenesis.";
RL   Mol. Cell. Biol. 27:6794-6805(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=19204925; DOI=10.1002/jemt.20696;
RA   Yu Y., Vanhorne J., Oko R.;
RT   "The origin and assembly of a zona pellucida binding protein, IAM38, during
RT   spermiogenesis.";
RL   Microsc. Res. Tech. 72:558-565(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Plays a role in acrosome compaction and sperm morphogenesis.
CC       Is implicated in sperm-oocyte interaction during fertilization.
CC       {ECO:0000269|PubMed:17664285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       membrane {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925};
CC       Peripheral membrane protein {ECO:0000305|PubMed:19204925}. Secreted
CC       {ECO:0000305}. Note=First localized in acrosome granule, later migrates
CC       to the inner and outer acrosomal membrane (PubMed:19204925). Released
CC       after the acrosomal reaction (PubMed:17664285).
CC       {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis (at protein level)
CC       (PubMed:19204925). Expressed in male germ cells (PubMed:17664285).
CC       {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}.
CC   -!- DEVELOPMENTAL STAGE: Barely detectable at 11 days postpartum (dpp),
CC       very strong signal from 20 dpp until adulthood (PubMed:19204925).
CC       Expressed from the mid-pachytene spermatocyte stage to the early
CC       elongating spermatid stage (PubMed:17664285, PubMed:19204925).
CC       {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17664285,
CC       ECO:0000269|PubMed:19204925}.
CC   -!- DISRUPTION PHENOTYPE: Male mice are infertile with abnormal round-
CC       headed sperm morphology and no forward sperm motility.
CC       {ECO:0000269|PubMed:17664285}.
CC   -!- SIMILARITY: Belongs to the zona pellucida-binding protein Sp38 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA04494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D17569; BAA04494.1; ALT_INIT; mRNA.
DR   EMBL; AK006274; BAB24497.1; -; mRNA.
DR   EMBL; AK018889; BAB31476.1; -; mRNA.
DR   EMBL; AK018921; BAB31483.1; -; mRNA.
DR   EMBL; AK029541; BAC26504.1; -; mRNA.
DR   RefSeq; NP_056600.1; NM_015785.2.
DR   AlphaFoldDB; Q62522; -.
DR   STRING; 10090.ENSMUSP00000020413; -.
DR   GlyGen; Q62522; 3 sites.
DR   PhosphoSitePlus; Q62522; -.
DR   PaxDb; Q62522; -.
DR   PRIDE; Q62522; -.
DR   ProteomicsDB; 275239; -.
DR   GeneID; 53604; -.
DR   KEGG; mmu:53604; -.
DR   CTD; 11055; -.
DR   MGI; MGI:1855701; Zpbp.
DR   eggNOG; ENOG502RJ20; Eukaryota.
DR   InParanoid; Q62522; -.
DR   OrthoDB; 1069241at2759; -.
DR   BioGRID-ORCS; 53604; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Zpbp; mouse.
DR   PRO; PR:Q62522; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q62522; protein.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
DR   GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR010857; Sp38-bd.
DR   PANTHER; PTHR15443; PTHR15443; 1.
DR   Pfam; PF07354; Sp38; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..350
FT                   /note="Zona pellucida-binding protein 1"
FT                   /id="PRO_0000041599"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  39232 MW;  CABD14DAE1C76EE8 CRC64;
     MEALAPGRAP RGRRRAGASG SVLSPLSLAA VLLCALLRAP PAVGHLARLP RSIHLTQDSL
     KIVGSTHFPV SVYVMLHQKS PHVLCVTQRL RNTELVDPSF QWHGPKGKLV SENTTAQVTS
     TGSLIFQSFE ETMSGVYTCF LEYKPTVEES IKNLQLKYIV YAYREPRFYY QFTARYHAAP
     CNSIYNISFE KKLLQILSKL VLDLSCEISL IKSECHRVKM QRAGLQNELF FTFSVASIDT
     EKGSKPCTDH SCEASKRLSK AKNLIERFFI QQVEVLGKRA EPLPEIYYIE GTLQMVWVNR
     CFPGYGINVL KHPKCPECCV VCSPGSFNPR DGTHCLQCNN SLVYGAKTCM
 
 
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