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ABCB6_RAT
ID   ABCB6_RAT               Reviewed;         836 AA.
AC   O70595;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000305};
DE   AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000250|UniProtKB:Q9NP58};
DE            EC=7.6.2.5 {ECO:0000250|UniProtKB:Q9NP58};
DE   AltName: Full=Ubiquitously-expressed mammalian ABC half transporter;
GN   Name=Abcb6 {ECO:0000312|RGD:71077}; Synonyms=Umat;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Hepatocyte;
RX   PubMed=9705847; DOI=10.1006/bbrc.1998.9110;
RA   Hirsch-Ernst K.I., Gaini-Rahimi S., Ernst B.-P., Schmitz-Salue C.,
RA   Blume S., Kahl G.F.;
RT   "Molecular cDNA cloning and tissue distribution of mRNA encoding a novel
RT   ATP-binding cassette (ABC) half-transporter.";
RL   Biochem. Biophys. Res. Commun. 249:151-155(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16390497; DOI=10.1111/j.1365-2605.2005.00616.x;
RA   Melaine N., Satie A.-P., Lassurguere J., Desmots S., Jegou B., Samson M.;
RT   "Molecular cloning of several rat ABC transporters including a new ABC
RT   transporter, Abcb8, and their expression in rat testis.";
RL   Int. J. Androl. 29:392-399(2006).
RN   [4]
RP   GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=18160489; DOI=10.1152/ajpcell.00612.2006;
RA   Jalil Y.A., Ritz V., Jakimenko A., Schmitz-Salue C., Siebert H., Awuah D.,
RA   Kotthaus A., Kietzmann T., Ziemann C., Hirsch-Ernst K.I.;
RT   "Vesicular localization of the rat ATP-binding cassette half-transporter
RT   rAbcb6.";
RL   Am. J. Physiol. 294:C579-C590(2008).
CC   -!- FUNCTION: ATP-dependent transporter that catalyzes the transport of a
CC       broad-spectrum of porphyrins from the cytoplasm to the extracellular
CC       space through the plasma membrane or into the vesicle lumen (By
CC       similarity). May also function as an ATP-dependent importer of
CC       porphyrins from the cytoplasm into the mitochondria, in turn may
CC       participate in the de novo heme biosynthesis regulation and in the
CC       coordination of heme and iron homeostasis during phenylhydrazine stress
CC       (By similarity). May play a key role in the early steps of
CC       melanogenesis producing PMEL amyloid fibrils (By similarity). In vitro,
CC       it confers to cells a resistance to toxic metal such as arsenic and
CC       cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-
CC       38 and vincristin (By similarity). In addition may play a role in the
CC       transition metal homeostasis (PubMed:18160489).
CC       {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate;
CC         Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:456216; EC=7.6.2.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin
CC         III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:131725, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide
CC         a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58687, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP +
CC         coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate +
CC         protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out)
CC         + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:167478, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate +
CC         uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:167480, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate +
CC         uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:167479, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777;
CC         Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NP58}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58};
CC       Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58};
CC       Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC       {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18160489}. Late
CC       endosome membrane {ECO:0000269|PubMed:18160489}. Early endosome
CC       membrane {ECO:0000269|PubMed:18160489}. Secreted, extracellular exosome
CC       {ECO:0000250|UniProtKB:Q9NP58}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane
CC       {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane
CC       {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature
CC       erythrocytes and in exosomes released from reticulocytes during the
CC       final steps of erythroid maturation. Traffics from endoplasmic
CC       reticulum to Golgi during its glycans's maturation, therefrom is first
CC       targeted to the plasma membrane, and is rapidly internalized through
CC       endocytosis to be distributed to the limiting membrane of
CC       multivesicular bodies and lysosomes. Localized on the limiting membrane
CC       of early melanosomes of pigment cells (By similarity). Targeted to the
CC       endolysosomal compartment (PubMed:18160489).
CC       {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis
CC       by meiotic pachytene spermatocytes and post-meiotic early spermatids.
CC       {ECO:0000269|PubMed:16390497, ECO:0000269|PubMed:9705847}.
CC   -!- DOMAIN: Contains two independently folding units, the N-terminal
CC       transmembrane domain (residues 1-205) and the ABC-core domain (206-842)
CC       are respectively responsible for the lysosomal targeting and the ATPase
CC       activity. {ECO:0000250|UniProtKB:Q9NP58}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18160489}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
CC   -!- CAUTION: To date, the intracellular localization of ABCB6 is a matter
CC       of debate, with conflicting reports suggesting mitochondrial or
CC       endolysosomal localization, therefore questioning the requirement of
CC       ABCB6 in the mitochondrial import of porphyrins.
CC       {ECO:0000250|UniProtKB:Q9NP58}.
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DR   EMBL; AJ003004; CAA05793.1; -; mRNA.
DR   EMBL; BC085712; AAH85712.1; -; mRNA.
DR   PIR; JE0248; JE0248.
DR   RefSeq; NP_542149.1; NM_080582.1.
DR   AlphaFoldDB; O70595; -.
DR   SMR; O70595; -.
DR   STRING; 10116.ENSRNOP00000025627; -.
DR   PhosphoSitePlus; O70595; -.
DR   jPOST; O70595; -.
DR   PaxDb; O70595; -.
DR   PRIDE; O70595; -.
DR   Ensembl; ENSRNOT00000025627; ENSRNOP00000025627; ENSRNOG00000018697.
DR   GeneID; 140669; -.
DR   KEGG; rno:140669; -.
DR   UCSC; RGD:71077; rat.
DR   CTD; 10058; -.
DR   RGD; 71077; Abcb6.
DR   eggNOG; KOG0056; Eukaryota.
DR   GeneTree; ENSGT00940000156160; -.
DR   HOGENOM; CLU_000604_32_0_1; -.
DR   InParanoid; O70595; -.
DR   OMA; TDPWVRP; -.
DR   OrthoDB; 248727at2759; -.
DR   PhylomeDB; O70595; -.
DR   TreeFam; TF105194; -.
DR   Reactome; R-RNO-1369007; Mitochondrial ABC transporters.
DR   PRO; PR:O70595; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000018697; Expressed in pancreas and 19 other tissues.
DR   ExpressionAtlas; O70595; baseline and differential.
DR   Genevisible; O70595; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0036020; C:endolysosome membrane; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:RGD.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR   GO; GO:0005740; C:mitochondrial envelope; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0032585; C:multivesicular body membrane; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0015439; F:ABC-type heme transporter activity; ISO:RGD.
DR   GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0020037; F:heme binding; ISO:RGD.
DR   GO; GO:0046906; F:tetrapyrrole binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; ISS:UniProtKB.
DR   GO; GO:0042168; P:heme metabolic process; ISS:UniProtKB.
DR   GO; GO:0035351; P:heme transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015886; P:heme transport; ISO:RGD.
DR   GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISO:RGD.
DR   GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISS:UniProtKB.
DR   GO; GO:0043588; P:skin development; ISO:RGD.
DR   GO; GO:0033013; P:tetrapyrrole metabolic process; ISS:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR032410; MTABC_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF16185; MTABC_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW   Endosome; Golgi apparatus; Lysosome; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Secreted; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..836
FT                   /note="ATP-binding cassette sub-family B member 6"
FT                   /id="PRO_0000268679"
FT   TOPO_DOM        1..26
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..106
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..185
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        286..305
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        327..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        397
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        419..499
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        500..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        521..529
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TOPO_DOM        551..836
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          265..556
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          590..824
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..236
FT                   /note="Required for ATPase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   REGION          1..205
FT                   /note="Required for the lysosomal targeting"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   BINDING         599
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         623..634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DISULFID        8..26
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
SQ   SEQUENCE   836 AA;  93305 MW;  40EC2C32E865522B CRC64;
     MVTVGNYCEA EGPAGPAWTQ NGLSPCFFYT LVPSTLMTLG VLALVLVLPC RRREVPAGTE
     ELSWAAGPRV APYALQLSLA ILQMALPLAS LAGRVGTARG VRLPGYLLLA SVLESLASAC
     GLWLLVVERS QARQSLAMGV WMKFRHSLGL LLLWTVTFAA ENLVLVSWNS PQWWWSRADL
     GQQVQFGLWV LRYMTSGGLF ILGLWAPGLR PQSYTLHVNE EDQDGGRNQG RSTDPRSTWR
     DLGRKLRLLS GYLWPRGSPS LQLTVLLCMG LMGLDRALNV LVPIFYRDIV NLLTSKAPWS
     SLAWTVTTYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRGVELRLF SHLHELSLRW
     HLGRRTGEVL RIVDRGTSSV TGLLSYLVFN IIPTLADIII GIIYFSMFFN AWFGLIVFLC
     MSLYLILTIM VTEWRAKFRR DMNTQENATR ARAVDSLLNF ETVKYYNAEG YELERYREAI
     LKFQGLEWKS TASLVLLNQT QNMVIGFGLL AGSLLCAYFV SERRLQVGDF VLFGTYITQL
     YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDVPGA GPLRFHKGRV EFENVHFSYA
     DGRETLQDVS FTVMPGQTVA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQI
     SLRSHIGVVP QDTVLFNDTI ANNIRYGRVT AGDSEIQAAA QAAGIHDAIL SFPEGYETQV
     GERGLKLSGG EKQRVAIART ILKAPDIILL DEATSALDTS NERAIQASLA KVCTNRTTIV
     VAHRLSTVVN ADQILVIKDG CIIERGRHEA LLSRGGVYAE MWQLQQQGQE TVPEDS
 
 
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