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LYZL4_RAT
ID   LYZL4_RAT               Reviewed;         145 AA.
AC   D4ABW7;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Lysozyme-like protein 4;
DE            Short=Lysozyme-4;
DE   Flags: Precursor;
GN   Name=Lyzl4; Synonyms=Lyza {ECO:0000303|PubMed:26862561};
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   SUBCELLULAR LOCATION, AND ABSENCE OF BACTERIOLYTIC AND LYSOZYME ACTIVITIES.
RC   STRAIN=Wistar; TISSUE=Epididymis;
RX   PubMed=22110709; DOI=10.1371/journal.pone.0027659;
RA   Narmadha G., Muneswararao K., Rajesh A., Yenugu S.;
RT   "Characterization of a novel lysozyme-like 4 gene in the rat.";
RL   PLoS ONE 6:E27659-E27659(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
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   [4]
RP   IDENTIFICATION.
RX   PubMed=26862561; DOI=10.1016/j.dib.2015.11.056;
RA   Premzl M.;
RT   "Curated eutherian third party data gene data sets.";
RL   Data Brief 6:208-213(2016).
CC   -!- FUNCTION: May be involved in fertilization (By similarity). Has no
CC       detectable bacteriolytic and lysozyme activities in vitro
CC       (PubMed:22110709). {ECO:0000250|UniProtKB:Q9D925,
CC       ECO:0000269|PubMed:22110709}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9D925}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9D925}.
CC       Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:Q9D925}. Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:22110709}. Note=Found in the principal piece of
CC       sperm tail. {ECO:0000250|UniProtKB:Q9D925,
CC       ECO:0000269|PubMed:22110709}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, lung, ovary, uterus and
CC       testis (PubMed:22110709). In testis expressed in the germinal
CC       epithelium and on the maturing spermatozoa (at protein level)
CC       (PubMed:22110709). {ECO:0000269|PubMed:22110709}.
CC   -!- DEVELOPMENTAL STAGE: Present during stages of postnatal development
CC       from 10 to 60 days old (PubMed:22110709).
CC       {ECO:0000269|PubMed:22110709}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC   -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Gly-
CC       72 is present instead of the conserved Asp which is an active site
CC       residue. It is therefore expected that this protein lacks hydrolase
CC       activity. {ECO:0000305}.
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DR   EMBL; HM125534; ADK94117.1; -; mRNA.
DR   EMBL; AABR07071764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473954; EDL76834.1; -; Genomic_DNA.
DR   EMBL; HG931781; CDM98782.1; -; Genomic_DNA.
DR   RefSeq; NP_001233112.1; NM_001246183.1.
DR   RefSeq; XP_006244187.1; XM_006244125.3.
DR   AlphaFoldDB; D4ABW7; -.
DR   SMR; D4ABW7; -.
DR   STRING; 10116.ENSRNOP00000026173; -.
DR   PaxDb; D4ABW7; -.
DR   Ensembl; ENSRNOT00000026173; ENSRNOP00000026173; ENSRNOG00000019350.
DR   GeneID; 363168; -.
DR   KEGG; rno:363168; -.
DR   UCSC; RGD:1308401; rat.
DR   CTD; 131375; -.
DR   RGD; 1308401; Lyzl4.
DR   eggNOG; ENOG502SSER; Eukaryota.
DR   GeneTree; ENSGT00940000162293; -.
DR   HOGENOM; CLU_111620_1_1_1; -.
DR   InParanoid; D4ABW7; -.
DR   OMA; AWPSWSL; -.
DR   OrthoDB; 1551203at2759; -.
DR   PhylomeDB; D4ABW7; -.
DR   TreeFam; TF324882; -.
DR   PRO; PR:D4ABW7; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Proteomes; UP000234681; Chromosome 8.
DR   Bgee; ENSRNOG00000019350; Expressed in testis and 3 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IBA:GO_Central.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR030062; LYZL4.
DR   PANTHER; PTHR11407; PTHR11407; 1.
DR   PANTHER; PTHR11407:SF21; PTHR11407:SF21; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasmic vesicle; Disulfide bond;
KW   Fertilization; Flagellum; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..145
FT                   /note="Lysozyme-like protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5008161378"
FT   DOMAIN          20..145
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        25..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        49..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        84..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        91..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   145 AA;  16302 MW;  130FF4FCACC68E6A CRC64;
     MQLYLVLLLI SYLLTPIGAS ILGRCVVAKK LYDGGLNYFE GYSLENWVCL AYFESKFNPS
     AVYENSRDGS TGFGLFQIRD NEWCDHGKNL CSVSCTALLN PNLKDTIECA KKIVKGKQGM
     GAWPVWSRNC QLSDILDRWL DGCEL
 
 
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