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COPT1_PONAB
ID   COPT1_PONAB             Reviewed;         190 AA.
AC   Q5RAS6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=High affinity copper uptake protein 1;
DE   AltName: Full=Copper transporter 1;
DE   AltName: Full=Solute carrier family 31 member 1;
GN   Name=SLC31A1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: High-affinity, saturable copper transporter involved in
CC       dietary copper uptake. {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=Localizes to the apical membrane in intestinal epithelial cells.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family.
CC       SLC31A subfamily. {ECO:0000305}.
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DR   EMBL; CR858936; CAH91134.1; -; mRNA.
DR   RefSeq; NP_001125663.1; NM_001132191.1.
DR   AlphaFoldDB; Q5RAS6; -.
DR   BMRB; Q5RAS6; -.
DR   SMR; Q5RAS6; -.
DR   STRING; 9601.ENSPPYP00000021867; -.
DR   GeneID; 100172583; -.
DR   KEGG; pon:100172583; -.
DR   CTD; 1317; -.
DR   eggNOG; KOG3386; Eukaryota.
DR   InParanoid; Q5RAS6; -.
DR   OrthoDB; 1389393at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005375; F:copper ion transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR007274; Cop_transporter.
DR   PANTHER; PTHR12483; PTHR12483; 1.
DR   Pfam; PF04145; Ctr; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Copper; Copper transport; Glycoprotein; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..190
FT                   /note="High affinity copper uptake protein 1"
FT                   /id="PRO_0000290192"
FT   TOPO_DOM        1..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         114
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O15431"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  21110 MW;  73431BBFCDED3EFE CRC64;
     MDHSHHMGMS YMDSNSTMQP SHHHPTTSAS HSRGGGDSSM MMMPMTFYFG FKNVELLFSG
     LVINTAGEMA GAFVAVFLLA MFYEGLKIAR ESLLRKSQVS IRYNSMPVPG PNGTILMETH
     KTVGQQMLSF PHLLQTVLHI IQVVISYFLM LIFMTYNGYL CIAVAAGAGT GYFLFSWKKA
     VVVDITEHCH
 
 
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