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ZPT71_CAEEL
ID   ZPT71_CAEEL             Reviewed;         393 AA.
AC   Q9XUC4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Zinc transporter zipt-7.1 {ECO:0000305};
DE   AltName: Full=Histidine-rich membrane protein KE4 homolog 1 {ECO:0000305};
GN   Name=zipt-7.1 {ECO:0000303|PubMed:29879108, ECO:0000312|WormBase:T28F3.3};
GN   Synonyms=hke-4.1 {ECO:0000312|WormBase:T28F3.3};
GN   ORFNames=T28F3.3 {ECO:0000312|WormBase:T28F3.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   INDUCTION.
RX   DOI=10.1093/icb/45.1.61;
RA   Novillo A., Won S.-J., Li C., Callard I.P.;
RT   "Changes in nuclear receptor and vitellogenin gene expression in response
RT   to steroids and heavy metal in Caenorhabditis elegans.";
RL   Integr. Comp. Biol. 45:61-71(2005).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF GLY-266.
RX   PubMed=29879108; DOI=10.1371/journal.pbio.2005069;
RA   Zhao Y., Tan C.H., Krauchunas A., Scharf A., Dietrich N., Warnhoff K.,
RA   Yuan Z., Druzhinina M., Gu S.G., Miao L., Singson A., Ellis R.E.,
RA   Kornfeld K.;
RT   "The zinc transporter ZIPT-7.1 regulates sperm activation in nematodes.";
RL   PLoS Biol. 16:E2005069-E2005069(2018).
CC   -!- FUNCTION: Zinc transporter which regulates intracellular zinc levels
CC       (PubMed:29879108). Required for spermatogenesis in both hermaphrodites
CC       and males where it resides in an inactive form in immature sperm,
CC       spermatids, but is likely activated in response to reduced spe-4 and
CC       spe-6 function (PubMed:29879108). Upon activation, mediates the release
CC       of zinc from internal stores in spermatids into the cytoplasm
CC       (PubMed:29879108). The resulting increase in cytoplasmic zinc levels
CC       promotes spermatid activation and subsequent differentiation into
CC       mature motile sperm that are capable of fertilization
CC       (PubMed:29879108). {ECO:0000269|PubMed:29879108}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:29879108}; Multi-
CC       pass membrane protein {ECO:0000305}. Note=Localizes to membranous
CC       organelles. {ECO:0000269|PubMed:29879108}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in developing spermatids (at the
CC       protein level) (PubMed:29879108). Expressed in the germline
CC       (PubMed:29879108). {ECO:0000269|PubMed:29879108}.
CC   -!- INDUCTION: By cholesterol. {ECO:0000269|Ref.2}.
CC   -!- DISRUPTION PHENOTYPE: Reduced brood size, but the majority of
CC       hermaphrodites are sterile and lay a large number of unfertilized
CC       oocytes (PubMed:29879108). Defective spermatid activation
CC       (PubMed:29879108). Double knockout with spe-4 results in failed
CC       spermatocyte division (PubMed:29879108). Double knockout with spe-6
CC       results in suppression of the premature spermatid activation phenotype
CC       of the single spe-6 (hc163) mutant (PubMed:29879108).
CC       {ECO:0000269|PubMed:29879108}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       KE4/Catsup subfamily. {ECO:0000305}.
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DR   EMBL; BX284604; CAB05297.2; -; Genomic_DNA.
DR   PIR; T25420; T25420.
DR   RefSeq; NP_503070.2; NM_070669.3.
DR   AlphaFoldDB; Q9XUC4; -.
DR   BioGRID; 43585; 1.
DR   STRING; 6239.T28F3.3; -.
DR   TCDB; 2.A.5.4.18; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR   PaxDb; Q9XUC4; -.
DR   EnsemblMetazoa; T28F3.3.1; T28F3.3.1; WBGene00044067.
DR   EnsemblMetazoa; T28F3.3.2; T28F3.3.2; WBGene00044067.
DR   EnsemblMetazoa; T28F3.3.3; T28F3.3.3; WBGene00044067.
DR   GeneID; 178509; -.
DR   KEGG; cel:CELE_T28F3.3; -.
DR   CTD; 178509; -.
DR   WormBase; T28F3.3; CE36329; WBGene00044067; zipt-7.1.
DR   eggNOG; KOG2693; Eukaryota.
DR   GeneTree; ENSGT00940000160076; -.
DR   HOGENOM; CLU_015114_0_1_1; -.
DR   InParanoid; Q9XUC4; -.
DR   OMA; IKGGHCH; -.
DR   OrthoDB; 657777at2759; -.
DR   PhylomeDB; Q9XUC4; -.
DR   PRO; PR:Q9XUC4; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00044067; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
DR   GO; GO:1905516; P:positive regulation of fertilization; IMP:UniProtKB.
DR   GO; GO:0046662; P:regulation of oviposition; IMP:UniProtKB.
DR   GO; GO:0048515; P:spermatid differentiation; IMP:UniProtKB.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   1: Evidence at protein level;
KW   Differentiation; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Spermatogenesis; Transmembrane; Transmembrane helix; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..393
FT                   /note="Zinc transporter zipt-7.1"
FT                   /id="PRO_0000213696"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          142..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         266
FT                   /note="G->E: In as42; defects in egg-laying associated with
FT                   embryonic hatching within the mother (also called the bag
FT                   of worms phenotype)."
FT                   /evidence="ECO:0000269|PubMed:29879108"
SQ   SEQUENCE   393 AA;  43324 MW;  27ABE48FB79A92F9 CRC64;
     MRLQLVALLF ALVFNAFSHE HSHEHHHEGD GSEILTKVGW NDHSEELHDH HEHDHDHHDE
     QLIRKNHTSH REIQHSRLST LKVWVFSLSA VVGISLAPCT LLFFIPAQHA NGPFLKILLA
     FGAGGLLGDA LLHIIPHSLS PHDHSHDHHD HNHSHKEHDH SHDHSNQLRV GTFVIAGILV
     FMMVEQLVRI IKGGHCHSHE NGHIVADEHR HLNEHDHEHS EEKKQQVEGL KDVKASAYLN
     LVADFVHNVT DGLAIGASFS AGNTLGWITT LTVLLHELPH EVGDFAILVQ SGFSKYQAIR
     LQAVTALGAI TGCVFSLLVS NPGSLNNDAD TSAIMPFTAG GFIYIATVSV VPELLESGDH
     NNLSKVAKMA QSLVHVLAIC MGVGMMYIVS LVE
 
 
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