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SCAM3_BOVIN
ID   SCAM3_BOVIN             Reviewed;         347 AA.
AC   Q58DR5; Q3ZCL2;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Secretory carrier-associated membrane protein 3;
DE            Short=Secretory carrier membrane protein 3;
GN   Name=SCAMP3;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC       recycling carrier to the cell surface (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NEDD4 and NEDD4L and TSG101. Interacts with
CC       RNF126. {ECO:0000250|UniProtKB:O14828, ECO:0000250|UniProtKB:O35609}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR   EMBL; BT021532; AAX46379.1; -; mRNA.
DR   EMBL; BC102055; AAI02056.1; -; mRNA.
DR   RefSeq; NP_001030503.1; NM_001035426.1.
DR   AlphaFoldDB; Q58DR5; -.
DR   SMR; Q58DR5; -.
DR   STRING; 9913.ENSBTAP00000044219; -.
DR   iPTMnet; Q58DR5; -.
DR   PaxDb; Q58DR5; -.
DR   PRIDE; Q58DR5; -.
DR   GeneID; 539670; -.
DR   KEGG; bta:539670; -.
DR   CTD; 10067; -.
DR   eggNOG; KOG3088; Eukaryota.
DR   InParanoid; Q58DR5; -.
DR   OrthoDB; 995882at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; PTHR10687; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   2: Evidence at transcript level;
KW   Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..347
FT                   /note="Secretory carrier-associated membrane protein 3"
FT                   /id="PRO_0000191256"
FT   TOPO_DOM        1..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..347
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         41
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         53
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   MOD_RES         83
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O35609"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   CROSSLNK        313
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:O14828"
FT   CONFLICT        121
FT                   /note="Q -> R (in Ref. 2; AAI02056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="S -> F (in Ref. 2; AAI02056)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  38278 MW;  A42981CD536E2F48 CRC64;
     MAQGRDGGNP FAEPGELDNP FQDPAVIQHR PSTHYATLDV YNPFETREPP PSYEPPAPVP
     IAPPSAPPLQ SSRKLSPTEP KNYGSYSTQA STAAATAELL KKQEELNRKA EELDRREREL
     QHAALGSTAT RQNNWPPLPS FCPVQPCFFQ DISMEIPQEF QKTVSTMYYL WMCSTLALLL
     NFLACLASFC VETSNGSGFG LSILWILLFT PCSFVCWYRP MYKAFRSDSS SNFFVFFFIF
     FVQDVLFVLQ AIGIPGWGFS GWISALVVLK VNTAVAVLML LVALFFTGIA VLGIVMLKRI
     HSLYRRTGAS FQKAQQEFAA GVFSNPAVRT AAANAAAGAA ENAFRAP
 
 
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