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PATE4_MOUSE
ID   PATE4_MOUSE             Reviewed;          99 AA.
AC   Q09098; Q9D248; Q9R018;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Prostate and testis expressed protein 4;
DE   AltName: Full=Calcium transport inhibitor;
DE   AltName: Full=Caltrin;
DE   AltName: Full=PATE-like protein B;
DE            Short=PATE-B;
DE   AltName: Full=Seminal vesicle protein 7;
DE   AltName: Full=Seminal vesicle protein VII;
DE            Short=SVS VII;
DE   Flags: Precursor;
GN   Name=Pate4; Synonyms=Svs7;
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], PROTEIN SEQUENCE OF 24-41, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=CD-1; TISSUE=Seminal vesicle;
RX   PubMed=11118436; DOI=10.1074/jbc.m006954200;
RA   Luo C.-W., Lin H.-J., Chen Y.-H.;
RT   "A novel heat-labile phospholipid-binding protein, SVS VII, in mouse
RT   seminal vesicle as a sperm motility enhancer.";
RL   J. Biol. Chem. 276:6913-6921(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 24-99.
RC   TISSUE=Seminal vesicle;
RX   PubMed=1400406; DOI=10.1016/s0021-9258(19)36774-2;
RA   Coronel C.E., Winnica D.E., Novella M.L., Lardy H.A.;
RT   "Purification, structure, and characterization of caltrin proteins from
RT   seminal vesicle of the rat and mouse.";
RL   J. Biol. Chem. 267:20909-20915(1992).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=18387948; DOI=10.1074/jbc.m801454200;
RA   Levitin F., Weiss M., Hahn Y., Stern O., Papke R.L., Matusik R.,
RA   Nandana S.R., Ziv R., Pichinuk E., Salame S., Bera T., Vincent J., Lee B.,
RA   Pastan I., Wreschner D.H.;
RT   "PATE gene clusters code for multiple, secreted TFP/Ly-6/uPAR proteins that
RT   are expressed in reproductive and neuron-rich tissues and possess
RT   neuromodulatory activity.";
RL   J. Biol. Chem. 283:16928-16939(2008).
CC   -!- FUNCTION: Enhances sperm motility. Binds to calmodulin and inhibits
CC       calcium transport into spermatozoa. May modulate the function of
CC       nicotinic acetylcholine receptors. {ECO:0000269|PubMed:11118436}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in prostate, testis, eye, kidney and
CC       skeletal muscle. Expressed in the dorsal lobe of prostate. Not
CC       expressed in the ventral lobe of prostate.
CC       {ECO:0000269|PubMed:18387948}.
CC   -!- INDUCTION: By castration in the ventral lobe of prostate. This
CC       induction is suppressed by subsequent dihydroxytestosterone
CC       administration.
CC   -!- MASS SPECTROMETRY: Mass=8538.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11118436};
CC   -!- SIMILARITY: Belongs to the PATE family. {ECO:0000305}.
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DR   EMBL; AF134204; AAD55589.1; -; mRNA.
DR   EMBL; AK020540; BAB32129.1; -; mRNA.
DR   EMBL; CH466522; EDL25400.1; -; Genomic_DNA.
DR   EMBL; BC120764; AAI20765.1; -; mRNA.
DR   EMBL; BC120766; AAI20767.1; -; mRNA.
DR   CCDS; CCDS22967.1; -.
DR   RefSeq; NP_064660.2; NM_020264.4.
DR   AlphaFoldDB; Q09098; -.
DR   STRING; 10090.ENSMUSP00000034610; -.
DR   TCDB; 8.A.31.1.4; the ly-6 neurotoxin-like protein1 precursor (lynx1) family.
DR   PhosphoSitePlus; Q09098; -.
DR   PaxDb; Q09098; -.
DR   PeptideAtlas; Q09098; -.
DR   PRIDE; Q09098; -.
DR   ProteomicsDB; 287997; -.
DR   Antibodypedia; 50680; 19 antibodies from 10 providers.
DR   Ensembl; ENSMUST00000034610; ENSMUSP00000034610; ENSMUSG00000032099.
DR   GeneID; 56872; -.
DR   KEGG; mmu:56872; -.
DR   UCSC; uc009otk.2; mouse.
DR   CTD; 399968; -.
DR   MGI; MGI:1930790; Pate4.
DR   VEuPathDB; HostDB:ENSMUSG00000032099; -.
DR   eggNOG; ENOG502T2SA; Eukaryota.
DR   GeneTree; ENSGT00550000076001; -.
DR   HOGENOM; CLU_181650_0_0_1; -.
DR   InParanoid; Q09098; -.
DR   OMA; QGTCIAK; -.
DR   OrthoDB; 1613958at2759; -.
DR   PhylomeDB; Q09098; -.
DR   BioGRID-ORCS; 56872; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Pate4; mouse.
DR   PRO; PR:Q09098; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q09098; protein.
DR   Bgee; ENSMUSG00000032099; Expressed in seminal vesicle and 17 other tissues.
DR   Genevisible; Q09098; MM.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0030548; F:acetylcholine receptor regulator activity; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:MGI.
DR   GO; GO:0099601; P:regulation of neurotransmitter receptor activity; ISO:MGI.
DR   GO; GO:0009611; P:response to wounding; IDA:MGI.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR031710; DUF4723.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF15851; DUF4723; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calmodulin-binding; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:11118436,
FT                   ECO:0000269|PubMed:1400406"
FT   CHAIN           24..99
FT                   /note="Prostate and testis expressed protein 4"
FT                   /id="PRO_0000036175"
FT   DOMAIN          24..99
FT                   /note="UPAR/Ly6"
FT                   /evidence="ECO:0000305"
FT   DISULFID        26..52
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..37
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..70
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000255"
FT   CONFLICT        40
FT                   /note="S -> P (in Ref. 1; AAD55589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90..91
FT                   /note="CC -> FG (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="C -> M (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="Missing (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   99 AA;  11058 MW;  18D1EC94C3B01D87 CRC64;
     MNSVTKISTL LIVILSFLCF VEGLICNSCE KSRDSRCTMS QSRCVAKPGE SCSTVSHFVG
     TKHVYSKQMC SPQCKEKQLN TGKKLIYIMC CEKNLCNSF
 
 
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