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GDPD4_MACFA
ID   GDPD4_MACFA             Reviewed;         627 AA.
AC   Q95JR7; Q95K28;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 4;
DE            EC=3.1.-.-;
GN   Name=GDPD4; ORFNames=QtsA-10771, QtsA-10831;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-627.
RC   TISSUE=Testis;
RA   Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA   Sugano S.;
RT   "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT   libraries.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB62944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB63057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB069999; BAB62944.1; ALT_INIT; mRNA.
DR   EMBL; AB070112; BAB63057.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q95JR7; -.
DR   SMR; Q95JR7; -.
DR   STRING; 9541.XP_005579219.1; -.
DR   eggNOG; KOG2258; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   Pfam; PF03009; GDPD; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS51704; GP_PDE; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..627
FT                   /note="Glycerophosphodiester phosphodiesterase domain-
FT                   containing protein 4"
FT                   /id="PRO_0000251939"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..468
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        490..627
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          198..457
FT                   /note="GP-PDE"
FT   BINDING         230
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         232
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         245
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   627 AA;  72388 MW;  3BB5C1C331E7D753 CRC64;
     MLLFLWIETS NEYFNFDWVI FLGTGYWFYW SIFILSLAGI LTAYSSLLLL LGLLLLWEGI
     ELYLHLCHKI LILLVILPCV ILMFIICKFW KERWLVAGLS LQIFAPYVHL VSITVMVILF
     WPVAIYVARL EREVRMRRYR MTHSEKKRLK KCNVIARLRG LQVAVGLPFL LIFLSLCLMP
     LGIYSPCIQE KENLGPKPTL FGHRGAPMLG PENTMMSFEK AVEHGAHGLE TDVHLSYDRV
     PFLMHDFDLR RTTNIREVQP ESAFKNPATF SWDFLSTLNA GKWFVKPELK PFYNMKPLSK
     ADKERARNQS IPTLADLLTL AKKERKFVIF DLRGPPPRHP LRHTFVRQVV SVILASKIEQ
     HLIFWLPAHD RRYVRSMAPG FQHVGHLVSV KTLAKNNISI INVDYKKLFP NGLRDYKAAN
     IRINVYTINE PWLFSLAWCS RINSVTTDNI GLLSQLNHPH FFMTPKFYMF IWLLVDIISV
     LFIVAIFCFH WRRETIKEKL FETSSTLTDT QSRSENEEDL HIAMKPARVV ESPWTLAALY
     PALSKSGKEH QGRFNFAAPS KKLVPIKNAV TPLKPGKHDI QPPMPTTVFE LTQAPSRQAK
     SKATFQTTLP TLKVDKPTMP SVEVPYP
 
 
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