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PA24D_MOUSE
ID   PA24D_MOUSE             Reviewed;         825 AA.
AC   Q50L43; A2AQJ1; Q3TJC5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Cytosolic phospholipase A2 delta {ECO:0000305};
DE            Short=cPLA2-delta {ECO:0000303|PubMed:15866882};
DE            EC=3.1.1.4 {ECO:0000269|PubMed:15866882};
DE   AltName: Full=Phospholipase A2 group IVD;
GN   Name=Pla2g4d {ECO:0000312|MGI:MGI:1925640};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=15866882; DOI=10.1074/jbc.m413711200;
RA   Ohto T., Uozumi N., Hirabayashi T., Shimizu T.;
RT   "Identification of novel cytosolic phospholipase A(2)s, murine
RT   cPLA(2)delta, epsilon, and zeta, which form a gene cluster with
RT   cPLA(2)beta.";
RL   J. Biol. Chem. 280:24576-24583(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Calcium-dependent phospholipase A2 that selectively
CC       hydrolyzes glycerophospholipids in the sn-2 position (PubMed:15866882).
CC       Compared to its human ortholog, may have no preference for the fatty
CC       acid found at the sn-2 position (PubMed:15866882).
CC       {ECO:0000269|PubMed:15866882}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC         glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:Q86XP0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000250|UniProtKB:Q86XP0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC         Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC         Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:15866882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:15866882};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC   -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+).
CC       {ECO:0000269|PubMed:15866882}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=13.4 pmol/min/mg enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC         eicosatetraenoyl)-sn-glycero-3-phosphocholine as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:15866882};
CC         Vmax=8.1 pmol/min/mg enzyme with 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphocholine as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:15866882};
CC         Vmax=14.5 pmol/min/mg enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC         eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine as substrate (at
CC         37 degrees Celsius) {ECO:0000269|PubMed:15866882};
CC         Vmax=19.9 pmol/min/mg enzyme with 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphoethanolamine as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:15866882};
CC         Vmax=16.4 pmol/min/mg enzyme with 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine as substrate (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15866882};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000269|PubMed:15866882}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}.
CC       Membrane {ECO:0000305|PubMed:15866882}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:15866882}; Cytoplasmic side
CC       {ECO:0000305|PubMed:15866882}. Note=Translocates to perinuclear
CC       membranes that may correspond to endoplasmic reticulum or Golgi in a
CC       calcium-dependent fashion. {ECO:0000269|PubMed:15866882}.
CC   -!- TISSUE SPECIFICITY: Weakly or not expressed in most tissues. Detected
CC       in placenta of 17.5 dpc embryos. {ECO:0000269|PubMed:15866882}.
CC   -!- DOMAIN: The N-terminal C2 domain mediates the association with lipid
CC       membranes upon calcium binding. An additional second C2 domain may
CC       stand in between the C2 domain and the PLA2c domain.
CC       {ECO:0000250|UniProtKB:Q86XP0}.
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DR   EMBL; AB195276; BAD98152.1; -; mRNA.
DR   EMBL; AK167492; BAE39570.1; -; mRNA.
DR   EMBL; AK145985; BAE26807.1; -; mRNA.
DR   EMBL; AL844608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16617.1; -.
DR   RefSeq; NP_001019308.1; NM_001024137.1.
DR   AlphaFoldDB; Q50L43; -.
DR   SMR; Q50L43; -.
DR   STRING; 10090.ENSMUSP00000092252; -.
DR   iPTMnet; Q50L43; -.
DR   PhosphoSitePlus; Q50L43; -.
DR   PaxDb; Q50L43; -.
DR   PRIDE; Q50L43; -.
DR   ProteomicsDB; 294370; -.
DR   Antibodypedia; 23488; 77 antibodies from 22 providers.
DR   DNASU; 78390; -.
DR   Ensembl; ENSMUST00000094665; ENSMUSP00000092252; ENSMUSG00000070719.
DR   GeneID; 78390; -.
DR   KEGG; mmu:78390; -.
DR   UCSC; uc008lvh.1; mouse.
DR   CTD; 283748; -.
DR   MGI; MGI:1925640; Pla2g4d.
DR   VEuPathDB; HostDB:ENSMUSG00000070719; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   GeneTree; ENSGT01030000234606; -.
DR   HOGENOM; CLU_011663_0_0_1; -.
DR   InParanoid; Q50L43; -.
DR   OMA; NSSHPVW; -.
DR   OrthoDB; 302848at2759; -.
DR   PhylomeDB; Q50L43; -.
DR   TreeFam; TF325228; -.
DR   Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR   Reactome; R-MMU-1483166; Synthesis of PA.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 78390; 3 hits in 73 CRISPR screens.
DR   PRO; PR:Q50L43; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q50L43; protein.
DR   Bgee; ENSMUSG00000070719; Expressed in esophagus and 25 other tissues.
DR   Genevisible; Q50L43; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; ISS:UniProtKB.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Metal-binding; Reference proteome.
FT   CHAIN           1..825
FT                   /note="Cytosolic phospholipase A2 delta"
FT                   /id="PRO_0000247024"
FT   DOMAIN          14..133
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          281..825
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   ACT_SITE        370
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q86XP0"
FT   ACT_SITE        654
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P47712"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         339..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q86XP0"
FT   CONFLICT        222
FT                   /note="R -> G (in Ref. 2; BAE39570/BAE26807)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="E -> G (in Ref. 2; BAE39570/BAE26807)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   825 AA;  93042 MW;  257668A34FFA841B CRC64;
     MWSGDRRVGM ESLSPERLHG HPYQEEASVF CRLTVKILEA RSLPRADLLS QADPYVTVQL
     PTASGMKFKT QTVTNSSHPV WNETFSFLIQ SQVKNILELT IYDEDVITKD DICFKVSYDV
     SEILPGQLLQ KTFSLNPQGP EELDVELLME RTWDPPENLI TNNVLVAREL SHLDVSLDRA
     GNTAMAAGQD KLELELMLKG SYEDTQTFFP DTAFTFSFHY MRGQDTELNG YLRGPRNSGW
     NSDTSVTPFN VPLMSLAAGK EMTIDIPAMK APEGKLQLKT DCCPKELSVR LSYGLCPEEQ
     AFLSRRKKVV AAALKQALQL DEDLNEDEVP VVGINAEGGG MRAMISLYGH LLALQKLGLL
     DCVTYFSGIS GSTWTMAHLY RDPEWSQRDL EGPISHAREH VAKTLLKEFL PEHLASYRQT
     LKLREEQGYT VTVADLWGLV LESKLHGQVT DQKLSGQRAA LERGQNPLPL YLSLNVKENH
     LETLHFKEWV EFSPYEVGFL KYGGFVPSEL FGSEFFMGRL MKRLPESQIC FLEGIWSNLF
     SVNLMDIWYD ITYGKDSNNF PVDVRNSEKE FSGSAGTSSG VEAPWLESGT ALAQALKGFL
     TGRPFHQRSA NFLHGLQLHR DYCNQRHFST WADCNLDDTP NQLTPQDPQL CLIDAGCFMN
     SSCPSLFRPG RQVDLIISFN YNQSLPFKGL QQSEKYSRAR GLPFPRVEPS PEDHSQPQEC
     YLFSDPTCPE APVVLHFPLV NDSFRDHSAP GVRRSPDELK AGQVNLTGAA SPYFMYNMTY
     KNEDFDRLLQ LSDYNVQNNQ GTILQALRTV LKRRASETRP LGVKT
 
 
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