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LETM1_HUMAN
ID   LETM1_HUMAN             Reviewed;         739 AA.
AC   O95202; B4DED2; Q9UF65;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Mitochondrial proton/calcium exchanger protein {ECO:0000305};
DE   AltName: Full=Leucine zipper-EF-hand-containing transmembrane protein 1;
DE   Flags: Precursor;
GN   Name=LETM1 {ECO:0000312|HGNC:HGNC:6556};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10486213; DOI=10.1006/geno.1999.5881;
RA   Endele S., Fuhry M., Pak S.-J., Zabel B.U., Winterpacht A.;
RT   "LETM1, a novel gene encoding a putative EF-hand Ca(2+)-binding protein,
RT   flanks the Wolf-Hirschhorn syndrome (WHS) critical region and is deleted in
RT   most WHS patients.";
RL   Genomics 60:218-225(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Cerebellum, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Skin;
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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14706454; DOI=10.1016/j.ygeno.2003.08.013;
RA   Schlickum S., Moghekar A., Simpson J.C., Steglich C., O'Brien R.J.,
RA   Winterpacht A., Endele S.U.;
RT   "LETM1, a gene deleted in Wolf-Hirschhorn syndrome, encodes an
RT   evolutionarily conserved mitochondrial protein.";
RL   Genomics 83:254-261(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15138253; DOI=10.1074/jbc.m403607200;
RA   Nowikovsky K., Froschauer E.M., Zsurka G., Samaj J., Reipert S.,
RA   Kolisek M., Wiesenberger G., Schweyen R.J.;
RT   "The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+
RT   homeostasis with a potential role in the Wolf-Hirschhorn syndrome.";
RL   J. Biol. Chem. 279:30307-30315(2004).
RN   [7]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH BCS1L.
RX   PubMed=18628306; DOI=10.1242/jcs.026625;
RA   Tamai S., Iida H., Yokota S., Sayano T., Kiguchiya S., Ishihara N.,
RA   Hayashi J., Mihara K., Oka T.;
RT   "Characterization of the mitochondrial protein LETM1, which maintains the
RT   mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L.";
RL   J. Cell Sci. 121:2588-2600(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-597, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=19797662; DOI=10.1126/science.1175145;
RA   Jiang D., Zhao L., Clapham D.E.;
RT   "Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+
RT   antiporter.";
RL   Science 326:144-147(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   FUNCTION.
RX   PubMed=24898248; DOI=10.1074/jbc.m113.540898;
RA   De Marchi U., Santo-Domingo J., Castelbou C., Sekler I., Wiederkehr A.,
RA   Demaurex N.;
RT   "NCLX protein, but not LETM1, mediates mitochondrial Ca2+ extrusion,
RT   thereby limiting Ca2+-induced NAD(P)H production and modulating matrix
RT   redox state.";
RL   J. Biol. Chem. 289:20377-20385(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Mitochondrial proton/calcium antiporter that mediates proton-
CC       dependent calcium efflux from mitochondrion (PubMed:19797662). Crucial
CC       for the maintenance of mitochondrial tubular networks and for the
CC       assembly of the supercomplexes of the respiratory chain
CC       (PubMed:18628306). Required for the maintenance of the tubular shape
CC       and cristae organization (PubMed:18628306). In contrast to SLC8B1/NCLX,
CC       does not constitute the major factor for mitochondrial calcium
CC       extrusion (PubMed:24898248). {ECO:0000269|PubMed:18628306,
CC       ECO:0000269|PubMed:19797662, ECO:0000269|PubMed:24898248}.
CC   -!- ACTIVITY REGULATION: Inhibited by ruthenium red or its derivative
CC       Ru360. {ECO:0000269|PubMed:19797662}.
CC   -!- SUBUNIT: Homohexamer (By similarity). Can form 2 complexes: a major
CC       (300 kDa) and a minor complex (500-600 kDa) (PubMed:18628306).
CC       Interacts with BCS1L (PubMed:18628306). {ECO:0000250|UniProtKB:Q9Z2I0,
CC       ECO:0000269|PubMed:18628306}.
CC   -!- INTERACTION:
CC       O95202; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-1052895, EBI-11962084;
CC       O95202; P25788: PSMA3; NbExp=3; IntAct=EBI-1052895, EBI-348380;
CC       O95202; P36508: ZNF76; NbExp=3; IntAct=EBI-1052895, EBI-7254550;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14706454, ECO:0000269|PubMed:15138253,
CC       ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:19797662}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:14706454,
CC       ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:18628306}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O95202-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95202-2; Sequence=VSP_037814, VSP_037815, VSP_037816;
CC       Name=3;
CC         IsoId=O95202-3; Sequence=VSP_037815, VSP_037816;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the LETM1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB63769.2; Type=Erroneous translation; Note=Incomplete prediction of CDS at the C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF061025; AAD13138.1; -; mRNA.
DR   EMBL; AK293572; BAG57043.1; -; mRNA.
DR   EMBL; AK310563; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL133650; CAB63769.2; ALT_SEQ; mRNA.
DR   EMBL; BC014500; AAH14500.1; -; mRNA.
DR   EMBL; BC021208; AAH21208.1; -; mRNA.
DR   CCDS; CCDS3355.1; -. [O95202-1]
DR   PIR; T43494; T43494.
DR   RefSeq; NP_036450.1; NM_012318.2. [O95202-1]
DR   AlphaFoldDB; O95202; -.
DR   SMR; O95202; -.
DR   BioGRID; 110145; 230.
DR   IntAct; O95202; 50.
DR   MINT; O95202; -.
DR   STRING; 9606.ENSP00000305653; -.
DR   TCDB; 2.A.97.1.1; the mitochondrial inner membrane k(+)/h(+) and ca(2+)/h(+) exchanger (letm1) family.
DR   iPTMnet; O95202; -.
DR   MetOSite; O95202; -.
DR   PhosphoSitePlus; O95202; -.
DR   SwissPalm; O95202; -.
DR   BioMuta; LETM1; -.
DR   EPD; O95202; -.
DR   jPOST; O95202; -.
DR   MassIVE; O95202; -.
DR   MaxQB; O95202; -.
DR   PaxDb; O95202; -.
DR   PeptideAtlas; O95202; -.
DR   PRIDE; O95202; -.
DR   ProteomicsDB; 50710; -. [O95202-1]
DR   ProteomicsDB; 50711; -. [O95202-2]
DR   ProteomicsDB; 50712; -. [O95202-3]
DR   Antibodypedia; 2597; 266 antibodies from 30 providers.
DR   DNASU; 3954; -.
DR   Ensembl; ENST00000302787.3; ENSP00000305653.2; ENSG00000168924.15. [O95202-1]
DR   GeneID; 3954; -.
DR   KEGG; hsa:3954; -.
DR   MANE-Select; ENST00000302787.3; ENSP00000305653.2; NM_012318.3; NP_036450.1.
DR   UCSC; uc003gdv.3; human. [O95202-1]
DR   CTD; 3954; -.
DR   DisGeNET; 3954; -.
DR   GeneCards; LETM1; -.
DR   HGNC; HGNC:6556; LETM1.
DR   HPA; ENSG00000168924; Low tissue specificity.
DR   MalaCards; LETM1; -.
DR   MIM; 604407; gene.
DR   neXtProt; NX_O95202; -.
DR   OpenTargets; ENSG00000168924; -.
DR   Orphanet; 280; Wolf-Hirschhorn syndrome.
DR   PharmGKB; PA30335; -.
DR   VEuPathDB; HostDB:ENSG00000168924; -.
DR   eggNOG; KOG1043; Eukaryota.
DR   GeneTree; ENSGT00950000183167; -.
DR   HOGENOM; CLU_008958_2_1_1; -.
DR   InParanoid; O95202; -.
DR   OMA; EILHYYH; -.
DR   OrthoDB; 516860at2759; -.
DR   PhylomeDB; O95202; -.
DR   TreeFam; TF316321; -.
DR   PathwayCommons; O95202; -.
DR   Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR   Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR   SignaLink; O95202; -.
DR   SIGNOR; O95202; -.
DR   BioGRID-ORCS; 3954; 642 hits in 1084 CRISPR screens.
DR   ChiTaRS; LETM1; human.
DR   GeneWiki; LETM1; -.
DR   GenomeRNAi; 3954; -.
DR   Pharos; O95202; Tbio.
DR   PRO; PR:O95202; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O95202; protein.
DR   Bgee; ENSG00000168924; Expressed in mucosa of transverse colon and 180 other tissues.
DR   Genevisible; O95202; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR   GO; GO:0015369; F:calcium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0099093; P:calcium export from the mitochondrion; IDA:UniProtKB.
DR   GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR   GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR   GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; IMP:UniProtKB.
DR   GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; IMP:UniProtKB.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011685; LETM1-like.
DR   InterPro; IPR044202; LETM1/MDM38-like.
DR   InterPro; IPR033122; LETM1_RBD.
DR   PANTHER; PTHR14009; PTHR14009; 1.
DR   Pfam; PF07766; LETM1; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51758; LETM1_RBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Antiport; Calcium; Calcium transport;
KW   Coiled coil; Ion transport; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..115
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           116..739
FT                   /note="Mitochondrial proton/calcium exchanger protein"
FT                   /id="PRO_0000017694"
FT   TOPO_DOM        116..208
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I0"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..739
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2I0"
FT   DOMAIN          252..537
FT                   /note="Letm1 RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT   DOMAIN          663..698
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          718..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          115..136
FT                   /evidence="ECO:0000255"
FT   COILED          462..490
FT                   /evidence="ECO:0000255"
FT   COILED          537..627
FT                   /evidence="ECO:0000255"
FT   COILED          708..739
FT                   /evidence="ECO:0000255"
FT   BINDING         676
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         678
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         680
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         682
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         687
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         597
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..48
FT                   /note="MASILLRSCRGRAPARLPPPPRYTVPRGSPGDPAHLSCASTLGLRNCL ->
FT                   MRHTWPFR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037814"
FT   VAR_SEQ         292..294
FT                   /note="KIR -> QVL (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037815"
FT   VAR_SEQ         295..739
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037816"
SQ   SEQUENCE   739 AA;  83354 MW;  942E9138F299D94F CRC64;
     MASILLRSCR GRAPARLPPP PRYTVPRGSP GDPAHLSCAS TLGLRNCLNV PFGCCTPIHP
     VYTSSRGDHL GCWALRPECL RIVSRAPWTS TSVGFVAVGP QCLPVRGWHS SRPVRDDSVV
     EKSLKSLKDK NKKLEEGGPV YSPPAEVVVK KSLGQRVLDE LKHYYHGFRL LWIDTKIAAR
     MLWRILNGHS LTRRERRQFL RICADLFRLV PFLVFVVVPF MEFLLPVAVK LFPNMLPSTF
     ETQSLKEERL KKELRVKLEL AKFLQDTIEE MALKNKAAKG SATKDFSVFF QKIRETGERP
     SNEEIMRFSK LFEDELTLDN LTRPQLVALC KLLELQSIGT NNFLRFQLTM RLRSIKADDK
     LIAEEGVDSL NVKELQAACR ARGMRALGVT EDRLRGQLKQ WLDLHLHQEI PTSLLILSRA
     MYLPDTLSPA DQLKSTLQTL PEIVAKEAQV KVAEVEGEQV DNKAKLEATL QEEAAIQQEH
     REKELQKRSE VAKDFEPERV VAAPQRPGTE PQPEMPDTVL QSETLKDTAP VLEGLKEEEI
     TKEEIDILSD ACSKLQEQKK SLTKEKEELE LLKEDVQDYS EDLQEIKKEL SKTGEEKYVE
     ESKASKRLTK RVQQMIGQID GLISQLEMDQ QAGKLAPANG MPTGENVISV AELINAMKQV
     KHIPESKLTS LAAALDENKD GKVNIDDLVK VIELVDKEDV HISTSQVAEI VATLEKEEKV
     EEKEKAKEKA EKEVAEVKS
 
 
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