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RN148_BOVIN
ID   RN148_BOVIN             Reviewed;         303 AA.
AC   Q2TA44;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=RING finger protein 148;
DE   Flags: Precursor;
GN   Name=RNF148;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BC111122; AAI11123.1; -; mRNA.
DR   RefSeq; NP_001074205.1; NM_001080736.2.
DR   AlphaFoldDB; Q2TA44; -.
DR   SMR; Q2TA44; -.
DR   PRIDE; Q2TA44; -.
DR   GeneID; 538888; -.
DR   KEGG; bta:538888; -.
DR   CTD; 378925; -.
DR   InParanoid; Q2TA44; -.
DR   OrthoDB; 1487241at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Metal-binding; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..303
FT                   /note="RING finger protein 148"
FT                   /id="PRO_0000255251"
FT   TRANSMEM        186..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          65..167
FT                   /note="PA"
FT   ZN_FING         256..297
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  34067 MW;  4B6AD0A5D61C7A01 CRC64;
     MSLLRITSSA HSSASSRLWR LGIFLLLSLP DSKGKAIWTA HLNITFQVGS RLISELGESG
     VFGNHSPLER VSGVVVLPEG WNQNACNPMT NFSRPGQTDP WLALIERGGC TFTRKINVAA
     EKGANGVIIY NYPGTGNKVF PMSHQGTENI VAVMIGNLKG MELLHLIQKG VYVKIIIEVG
     RMHMPWLSHY IMSLFTFLTA TVAYLFLYCA WRPRGPNFST RRQRQLKADV RKAIGKLQLR
     VLQEGDKELE PDEDNCVVCF DIYKPQDVVR ILTCKHIFHK ACIDPWLLAH RTCPMCKCDI
     LQT
 
 
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