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NHEB_ONCMY
ID   NHEB_ONCMY              Reviewed;         759 AA.
AC   Q01345;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Na(+)/H(+) exchanger beta;
DE   AltName: Full=Beta-NHE;
DE   AltName: Full=Na(+)/H(+) antiporter;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Nucleated erythrocyte;
RX   PubMed=1379718; DOI=10.1073/pnas.89.15.6765;
RA   Borgese F., Sardet C., Cappadoro M., Pouyssegur J., Motais R.;
RT   "Cloning and expression of a cAMP-activated Na+/H+ exchanger: evidence that
RT   the cytoplasmic domain mediates hormonal regulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6765-6769(1992).
CC   -!- FUNCTION: Involved in pH regulation to eliminate acids generated by
CC       active metabolism or to counter adverse environmental conditions. Major
CC       proton extruding system driven by the inward sodium ion chemical
CC       gradient.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC       protein.
CC   -!- PTM: Activated by cAMP, protein kinase A and protein kinase C.
CC   -!- MISCELLANEOUS: Inhibited by amiloride and 5-amino-substituted
CC       derivatives and activated in a cooperative fashion by intracellular
CC       H(+).
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC       transporter (TC 2.A.36) family. {ECO:0000305}.
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DR   EMBL; M94581; AAA49549.1; -; mRNA.
DR   PIR; A46188; A46188.
DR   RefSeq; NP_001118167.1; NM_001124695.1.
DR   AlphaFoldDB; Q01345; -.
DR   SMR; Q01345; -.
DR   GeneID; 100136740; -.
DR   KEGG; omy:100136740; -.
DR   CTD; 795135; -.
DR   OrthoDB; 389547at2759; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IEA:InterPro.
DR   GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR004709; NaH_exchanger.
DR   InterPro; IPR001970; NHE-1-like.
DR   InterPro; IPR032103; NHE_CaM-bd.
DR   PANTHER; PTHR10110; PTHR10110; 1.
DR   PANTHER; PTHR10110:SF59; PTHR10110:SF59; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   Pfam; PF16644; NEXCaM_BD; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01085; NAHEXCHNGR1.
DR   TIGRFAMs; TIGR00840; b_cpa1; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..759
FT                   /note="Na(+)/H(+) exchanger beta"
FT                   /id="PRO_0000052369"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..34
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..95
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..117
FT                   /note="Helical; Name=M3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..142
FT                   /note="Helical; Name=M4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..169
FT                   /note="Helical; Name=M5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..214
FT                   /note="Helical; Name=M5A"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..244
FT                   /note="Helical; Name=M5B"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..261
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical; Name=M6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..330
FT                   /note="Helical; Name=M7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..372
FT                   /note="Helical; Name=M8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..376
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..398
FT                   /note="Helical; Name=M9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..446
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical; Name=M10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..759
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          681..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         641
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         648
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   759 AA;  85174 MW;  D6D95442995AE251 CRC64;
     MPAFSCAFPG CRRDLLVIVL VVFVGIGLPI EASAPAYQSH GTEGSHLTNI TNTKKAFPVL
     AVNYEHVRKP FEIALWILLA LLMKLGFHLI PRLSAVVPES CLLIVVGLLV GGLIKVIGEE
     PPVLDSQLFF LCLLPPIILD AGYFLPIRPF TENVGTILVF AVIGTLWNAF FMGGLLYALC
     QIESVGLSGV DLLACLLFGS IVSAVDPVAV LAVFEEIHIN ELVHILVFGE SLLNDAVTVV
     LYNLFEEFSK VGTVTVLDVF LGVVCFFVVS LGGVLVGAIY GFLAAFTSRF TSHTRVIEPL
     FVFLYSYMAY LSSEMFHLSG IMALIACGVV MRPYVEANIS HKSYTTIKYF LKMWSSVSET
     LIFIFLGVST VAGPHAWNWT FVITTVILCL VSRVLGVIGL TFIINKFRIV KLTKKDQFIV
     AYGGLRGAIA FSLGYLLSNS HQMRNLFLTA IITVIFFTVF VQGMTIRPLV ELLAVKKKKE
     SKPSINEEIH TEFLDHLLTG VEGVCGHYGH YHWKEKLNRF NKTYVKRWLI AGENFKEPEL
     IAFYRKMELK QAIMMVESGQ LPSVLPSTIS MQNIQPRAIP RVSKKREEEI RRILRANLQN
     NKQKMRSRSY SRHTLFDADE EDNVSEVRLR KTKMEMERRV SVMERRMSHY LTVPANRESP
     RPGVRRVRFE SDNQVFSADS FPTVHFEQPS PPSTPDAVSL EEEEEEVPKR PSLKADIEGP
     RGNASDNHQG ELDYQRLARC LSDPGPNKDK EDDDPFMSC
 
 
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