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TTL11_MOUSE
ID   TTL11_MOUSE             Reviewed;         727 AA.
AC   A4Q9F4; Q1LZJ9; Q9D4E7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tubulin polyglutamylase TTLL11 {ECO:0000303|PubMed:17499049};
DE            EC=6.3.2.- {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212};
DE   AltName: Full=Tubulin--tyrosine ligase-like protein 11;
GN   Name=Ttll11 {ECO:0000312|EMBL:CAM84332.1, ECO:0000312|MGI:MGI:1921660};
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:CAM84332.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:CAM84332.1};
RX   PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA   van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT   "A targeted multienzyme mechanism for selective microtubule
RT   polyglutamylation.";
RL   Mol. Cell 26:437-448(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-727 (ISOFORM 3).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB30318.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB30318.1};
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 MRNA] OF 185-727 (ISOFORM 2).
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   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20530212; DOI=10.1083/jcb.201001024;
RA   Lacroix B., van Dijk J., Gold N.D., Guizetti J., Aldrian-Herrada G.,
RA   Rogowski K., Gerlich D.W., Janke C.;
RT   "Tubulin polyglutamylation stimulates spastin-mediated microtubule
RT   severing.";
RL   J. Cell Biol. 189:945-954(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=23897886; DOI=10.1083/jcb.201305041;
RA   Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA   Giordano T., Spassky N., Janke C.;
RT   "Tubulin glycylases and glutamylases have distinct functions in
RT   stabilization and motility of ependymal cilia.";
RL   J. Cell Biol. 202:441-451(2013).
CC   -!- FUNCTION: Polyglutamylase which modifies tubulin, generating
CC       polyglutamate side chains of variable lengths on the gamma-carboxyl
CC       group of specific glutamate residues within the C-terminal tail of
CC       tubulin (PubMed:17499049, PubMed:20530212). Preferentially mediates
CC       ATP-dependent polyglutamate long side-chain elongation over the
CC       initiation step of the polyglutamylation reaction (PubMed:17499049,
CC       PubMed:20530212). Preferentially modifies the alpha-tubulin tail over a
CC       beta-tail (PubMed:17499049). Required for CCSAP localization to both
CC       spindle and cilia microtubules (By similarity). Promotes tubulin
CC       polyglutamylation which stimulates spastin/SPAST-mediated microtubule
CC       severing, thereby regulating microtubule functions (PubMed:20530212).
CC       {ECO:0000250|UniProtKB:Q8NHH1, ECO:0000269|PubMed:17499049,
CC       ECO:0000269|PubMed:20530212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC         glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC         Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC         Evidence={ECO:0000305|PubMed:17499049};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC         L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC         + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC         Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049,
CC         ECO:0000269|PubMed:20530212};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC         Evidence={ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:20530212};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton
CC       {ECO:0000305|PubMed:20530212}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:17499049};
CC         IsoId=A4Q9F4-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=A4Q9F4-2; Sequence=VSP_052719;
CC       Name=3 {ECO:0000269|PubMed:16141072};
CC         IsoId=A4Q9F4-3; Sequence=VSP_052718, VSP_052719;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, kidney, liver, lung,
CC       muscle and testis (PubMed:17499049). Expressed in heart, spleen and
CC       trachea (PubMed:17499049). In the brain, expressed in ependymal cilia,
CC       cortex, corpus callosum and striatum (PubMed:23897886).
CC       {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:23897886}.
CC   -!- DOMAIN: The flexible c-MTBD (cationic microtubule binding domain)
CC       region mediates binding to microtubules. It is positively charged and
CC       becomes ordered when bound to microtubules: it interacts with a
CC       negatively charged patch on tubulin. The presence of positive charges
CC       in the c-MTBD region is essential for proper binding.
CC       {ECO:0000250|UniProtKB:Q6ZT98, ECO:0000250|UniProtKB:Q8NHH1}.
CC   -!- DOMAIN: Gln-252 is the main determinant for regioselectivity, which
CC       segregates between initiases and elongases in all tubulin--tyrosine
CC       ligase family. A glutamine residue at this position is found in
CC       elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC       chain elongation, whereas an arginine residue is found in initiases
CC       TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC       {ECO:0000250|UniProtKB:A4Q9E8}.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30318.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB30318.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB30318.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AM690755; CAM84332.1; -; mRNA.
DR   EMBL; AK016577; BAB30318.1; ALT_SEQ; mRNA.
DR   EMBL; BC115858; AAI15859.1; -; mRNA.
DR   CCDS; CCDS50579.1; -. [A4Q9F4-1]
DR   RefSeq; NP_084050.1; NM_029774.2. [A4Q9F4-1]
DR   AlphaFoldDB; A4Q9F4; -.
DR   SMR; A4Q9F4; -.
DR   BioGRID; 216728; 1.
DR   STRING; 10090.ENSMUSP00000028248; -.
DR   PhosphoSitePlus; A4Q9F4; -.
DR   PaxDb; A4Q9F4; -.
DR   PRIDE; A4Q9F4; -.
DR   ProteomicsDB; 300049; -. [A4Q9F4-1]
DR   ProteomicsDB; 300050; -. [A4Q9F4-2]
DR   ProteomicsDB; 300051; -. [A4Q9F4-3]
DR   Antibodypedia; 53016; 16 antibodies from 8 providers.
DR   Ensembl; ENSMUST00000028248; ENSMUSP00000028248; ENSMUSG00000026885. [A4Q9F4-1]
DR   Ensembl; ENSMUST00000112976; ENSMUSP00000108600; ENSMUSG00000026885. [A4Q9F4-2]
DR   GeneID; 74410; -.
DR   KEGG; mmu:74410; -.
DR   UCSC; uc008jkz.3; mouse. [A4Q9F4-1]
DR   CTD; 158135; -.
DR   MGI; MGI:1921660; Ttll11.
DR   VEuPathDB; HostDB:ENSMUSG00000026885; -.
DR   eggNOG; KOG2158; Eukaryota.
DR   GeneTree; ENSGT00940000156689; -.
DR   HOGENOM; CLU_010131_6_0_1; -.
DR   InParanoid; A4Q9F4; -.
DR   OMA; SAPDCNA; -.
DR   OrthoDB; 1251554at2759; -.
DR   PhylomeDB; A4Q9F4; -.
DR   TreeFam; TF313087; -.
DR   BRENDA; 6.3.2.B3; 3474.
DR   Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   BioGRID-ORCS; 74410; 3 hits in 70 CRISPR screens.
DR   ChiTaRS; Ttll11; mouse.
DR   PRO; PR:A4Q9F4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A4Q9F4; protein.
DR   Bgee; ENSMUSG00000026885; Expressed in gastrula and 118 other tissues.
DR   ExpressionAtlas; A4Q9F4; baseline and differential.
DR   Genevisible; A4Q9F4; MM.
DR   GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051013; P:microtubule severing; IDA:MGI.
DR   GO; GO:0018095; P:protein polyglutamylation; IDA:MGI.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW   Cytoskeleton; Ligase; Magnesium; Metal-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..727
FT                   /note="Tubulin polyglutamylase TTLL11"
FT                   /id="PRO_0000326165"
FT   DOMAIN          125..477
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..343
FT                   /note="L-glutamate"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   REGION          464..566
FT                   /note="c-MTBD region"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHH1"
FT   REGION          530..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         252..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         252
FT                   /ligand="a protein"
FT                   /ligand_id="ChEBI:CHEBI:16541"
FT                   /ligand_part="L-glutamate residue"
FT                   /ligand_part_id="ChEBI:CHEBI:29973"
FT                   /ligand_part_note="L-glutamate acceptor residue in protein
FT                   target"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         279..282
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         292..294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         318
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         340..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         362
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         440
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         470
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   SITE            252
FT                   /note="Essential for specifying alpha-elongation versus
FT                   initiation step of the polyglutamylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   VAR_SEQ         210..281
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052718"
FT   VAR_SEQ         491..524
FT                   /note="HFPDIYMDRKHRIPPVSDRMSSWKHKGSSLSIVR -> Q (in isoform
FT                   2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052719"
FT   CONFLICT        110
FT                   /note="R -> G (in Ref. 2; BAB30318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="S -> G (in Ref. 2; BAB30318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="S -> D (in Ref. 2; BAB30318)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   727 AA;  82361 MW;  661A7FB585BB9EDB CRC64;
     MRRSSPEKKP EAEWEADAAA AAAATAAATE SLPAETEKQQ GVDAGAAGDP ERLELEEQPK
     DVGRIPTPTR RHAPEEGEAR VVRRLPPALP LAQPRPAARA LSQLVKARGR SRSRVYRRSA
     GSMRPVTVDS SKARTSLDAL KISLRQLRWK EFPFGRRLPC DIYWHGVSFR DSDILSGQVN
     KFPGMTEMVR KVTLSRALRI MQNLFPEEYN FYPRSWILPE EFQLFVSQVQ TVKEGDPSWK
     PTFIVKPDSG CQGDGIYLIK DPCDGRLTGT LHNRPAVVQE YIRKPLLIDK LKFDIRLYVL
     LKSLDPLEIY IAKDGLSRFC TEPYQEPNPQ NLHHVFMHLT NYSLNIHSGK FVHSDSASTG
     SKRTFSSILC RLSSKGVDIK KVWSDIISLV IKTVIALTPE LKVFYQSDIP TGRPGPTCFQ
     ILGFDILLMK NLKPMLLEVN ANPSMRIEHE YELSPGVFEN IPSLVDEEVK VAVIRDTLRL
     MDPLKKKKEI HFPDIYMDRK HRIPPVSDRM SSWKHKGSSL SIVRSQQMEK SFTSKEDLNC
     DPTGGDSEPN PEAHLPSICL KQVFPKYAKQ FNYLRLVDRM ANLFIRFLGI KGTMKLGPTG
     FRTFIRNCKL SSSSLSMAAV DILYIDITRR WNSVTVDQRD SGMCLQAFVE AFFFLAQRKF
     KLQPLHEQVA SLIDLCEYHL SVLDEKRLLC HRGRPLQRNP PQMNRPEHSA TGSSAPRVIG
     ASKLSQS
 
 
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