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SAXO1_HUMAN
ID   SAXO1_HUMAN             Reviewed;         474 AA.
AC   Q8IYX7; A8K880; Q5VY58;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Stabilizer of axonemal microtubules 1 {ECO:0000303|PubMed:25673876};
GN   Name=SAXO1; Synonyms=C9orf138, FAM154A;
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 [LARGE SCALE MRNA], AND VARIANTS GLU-27 AND SER-63.
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-27 AND
RP   SER-63.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-27 AND SER-63.
RC   TISSUE=Brain;
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   FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBUNIT, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   116-ARG--PRO-119.
RX   PubMed=25673876; DOI=10.1242/jcs.155143;
RA   Dacheux D., Roger B., Bosc C., Landrein N., Roche E., Chansel L., Trian T.,
RA   Andrieux A., Papaxanthos-Roche A., Marthan R., Robinson D.R., Bonhivers M.;
RT   "Human FAM154A (SAXO1) is a microtubule-stabilizing protein specific to
RT   cilia and related structures.";
RL   J. Cell Sci. 128:1294-1307(2015).
CC   -!- FUNCTION: May play a role in the regulation of cilium length.
CC       Stabilizes microtubules at low temperature.
CC       {ECO:0000269|PubMed:25673876}.
CC   -!- SUBUNIT: Associates with microtubules via the Mn regions.
CC       {ECO:0000269|PubMed:25673876}.
CC   -!- INTERACTION:
CC       Q8IYX7; P35609: ACTN2; NbExp=7; IntAct=EBI-3957636, EBI-77797;
CC       Q8IYX7; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-3957636, EBI-357530;
CC       Q8IYX7; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-3957636, EBI-742909;
CC       Q8IYX7; O95429: BAG4; NbExp=3; IntAct=EBI-3957636, EBI-2949658;
CC       Q8IYX7; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-3957636, EBI-742722;
CC       Q8IYX7; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-3957636, EBI-11976299;
CC       Q8IYX7; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-3957636, EBI-11530605;
CC       Q8IYX7; P55273: CDKN2D; NbExp=3; IntAct=EBI-3957636, EBI-745859;
CC       Q8IYX7; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-3957636, EBI-749051;
CC       Q8IYX7; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-3957636, EBI-2555370;
CC       Q8IYX7; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-3957636, EBI-12012272;
CC       Q8IYX7; P46108: CRK; NbExp=3; IntAct=EBI-3957636, EBI-886;
CC       Q8IYX7; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3957636, EBI-3867333;
CC       Q8IYX7; Q86V42: FAM124A; NbExp=3; IntAct=EBI-3957636, EBI-744506;
CC       Q8IYX7; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-3957636, EBI-2510157;
CC       Q8IYX7; Q14192: FHL2; NbExp=4; IntAct=EBI-3957636, EBI-701903;
CC       Q8IYX7; Q13643: FHL3; NbExp=9; IntAct=EBI-3957636, EBI-741101;
CC       Q8IYX7; Q5TD97: FHL5; NbExp=3; IntAct=EBI-3957636, EBI-750641;
CC       Q8IYX7; P14136: GFAP; NbExp=3; IntAct=EBI-3957636, EBI-744302;
CC       Q8IYX7; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-3957636, EBI-748515;
CC       Q8IYX7; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-3957636, EBI-5460660;
CC       Q8IYX7; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-3957636, EBI-748420;
CC       Q8IYX7; O75031: HSF2BP; NbExp=3; IntAct=EBI-3957636, EBI-7116203;
CC       Q8IYX7; Q8NA54: IQUB; NbExp=3; IntAct=EBI-3957636, EBI-10220600;
CC       Q8IYX7; Q2TBA0: KLHL40; NbExp=3; IntAct=EBI-3957636, EBI-7851314;
CC       Q8IYX7; P25800: LMO1; NbExp=3; IntAct=EBI-3957636, EBI-8639312;
CC       Q8IYX7; P25791: LMO2; NbExp=4; IntAct=EBI-3957636, EBI-739696;
CC       Q8IYX7; P25791-3: LMO2; NbExp=3; IntAct=EBI-3957636, EBI-11959475;
CC       Q8IYX7; P45984: MAPK9; NbExp=3; IntAct=EBI-3957636, EBI-713568;
CC       Q8IYX7; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-3957636, EBI-11750983;
CC       Q8IYX7; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-3957636, EBI-10297093;
CC       Q8IYX7; O43482: OIP5; NbExp=3; IntAct=EBI-3957636, EBI-536879;
CC       Q8IYX7; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-3957636, EBI-9057006;
CC       Q8IYX7; Q99471: PFDN5; NbExp=3; IntAct=EBI-3957636, EBI-357275;
CC       Q8IYX7; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-3957636, EBI-949255;
CC       Q8IYX7; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-3957636, EBI-11339910;
CC       Q8IYX7; O15160: POLR1C; NbExp=3; IntAct=EBI-3957636, EBI-1055079;
CC       Q8IYX7; O60504: SORBS3; NbExp=3; IntAct=EBI-3957636, EBI-741237;
CC       Q8IYX7; O75716: STK16; NbExp=6; IntAct=EBI-3957636, EBI-749295;
CC       Q8IYX7; Q13470-2: TNK1; NbExp=3; IntAct=EBI-3957636, EBI-11018037;
CC       Q8IYX7; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-3957636, EBI-492476;
CC       Q8IYX7; Q15654: TRIP6; NbExp=3; IntAct=EBI-3957636, EBI-742327;
CC       Q8IYX7; Q548N1: VPS28; NbExp=3; IntAct=EBI-3957636, EBI-10243107;
CC       Q8IYX7; Q9UK41: VPS28; NbExp=3; IntAct=EBI-3957636, EBI-727424;
CC       Q8IYX7; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-3957636, EBI-12040603;
CC       Q8IYX7; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-3957636, EBI-12030590;
CC       Q8IYX7; Q96E35: ZMYND19; NbExp=6; IntAct=EBI-3957636, EBI-746595;
CC       Q8IYX7; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3957636, EBI-3957603;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000269|PubMed:25673876}. Cytoplasm,
CC       cytoskeleton, cilium basal body {ECO:0000269|PubMed:25673876}.
CC       Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25673876}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:25673876}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000269|PubMed:25673876}. Note=In multi-ciliated cells,
CC       localizes to the basal bodies and in non-ciliated cells, to the
CC       centrosome. In spermatozoa, colocalizes with microtubules along the
CC       length of the axoneme from its proximal end to its distal tip and with
CC       tubulin at the distal end of the flagellum and at the proximal
CC       centriole. {ECO:0000269|PubMed:25673876}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis.
CC       Expressed in mature spermatozoa (at protein level).
CC       {ECO:0000269|PubMed:25673876}.
CC   -!- DEVELOPMENTAL STAGE: In retinal pigment epithelium (RPE1) cell line,
CC       after 24 hours of serum starvation to stimulate primary cilium
CC       production, present at the mother and daughter basal bodies. At early
CC       time points of ciliogenesis, not detected in the axoneme. At later time
CC       points, expressed along the axoneme, with increasing levels as
CC       maturation of the cilium proceeds. {ECO:0000269|PubMed:25673876}.
CC   -!- DOMAIN: The Mn regions are involved in microtubule-binding and
CC       stabilization at low temperature. They are required and sufficient for
CC       cilium targeting. {ECO:0000269|PubMed:25673876}.
CC   -!- DOMAIN: The N-terminal region (residues 1-29) might play a role in
CC       centriole retention. {ECO:0000269|PubMed:25673876}.
CC   -!- SIMILARITY: Belongs to the FAM154 family. {ECO:0000305}.
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DR   EMBL; AK292245; BAF84934.1; -; mRNA.
DR   EMBL; AL158150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL356000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58654.1; -; Genomic_DNA.
DR   EMBL; BC033489; AAH33489.1; -; mRNA.
DR   CCDS; CCDS6487.1; -.
DR   RefSeq; NP_001273978.1; NM_001287049.1.
DR   RefSeq; NP_001273979.1; NM_001287050.1.
DR   RefSeq; NP_714918.2; NM_153707.3.
DR   AlphaFoldDB; Q8IYX7; -.
DR   BioGRID; 127666; 53.
DR   IntAct; Q8IYX7; 49.
DR   STRING; 9606.ENSP00000369907; -.
DR   iPTMnet; Q8IYX7; -.
DR   PhosphoSitePlus; Q8IYX7; -.
DR   BioMuta; SAXO1; -.
DR   DMDM; 73620045; -.
DR   MassIVE; Q8IYX7; -.
DR   PaxDb; Q8IYX7; -.
DR   PeptideAtlas; Q8IYX7; -.
DR   PRIDE; Q8IYX7; -.
DR   ProteomicsDB; 71259; -.
DR   Antibodypedia; 10233; 45 antibodies from 15 providers.
DR   DNASU; 158297; -.
DR   Ensembl; ENST00000380534.9; ENSP00000369907.4; ENSG00000155875.15.
DR   GeneID; 158297; -.
DR   KEGG; hsa:158297; -.
DR   MANE-Select; ENST00000380534.9; ENSP00000369907.4; NM_153707.4; NP_714918.2.
DR   UCSC; uc003zni.4; human.
DR   CTD; 158297; -.
DR   DisGeNET; 158297; -.
DR   GeneCards; SAXO1; -.
DR   HGNC; HGNC:28566; SAXO1.
DR   HPA; ENSG00000155875; Tissue enriched (testis).
DR   MIM; 616292; gene.
DR   neXtProt; NX_Q8IYX7; -.
DR   OpenTargets; ENSG00000155875; -.
DR   PharmGKB; PA162386652; -.
DR   VEuPathDB; HostDB:ENSG00000155875; -.
DR   eggNOG; ENOG502QWHB; Eukaryota.
DR   GeneTree; ENSGT00390000007252; -.
DR   HOGENOM; CLU_047658_0_0_1; -.
DR   InParanoid; Q8IYX7; -.
DR   OMA; TTAQAHY; -.
DR   OrthoDB; 732196at2759; -.
DR   PhylomeDB; Q8IYX7; -.
DR   TreeFam; TF319394; -.
DR   PathwayCommons; Q8IYX7; -.
DR   SignaLink; Q8IYX7; -.
DR   BioGRID-ORCS; 158297; 12 hits in 1070 CRISPR screens.
DR   ChiTaRS; SAXO1; human.
DR   GenomeRNAi; 158297; -.
DR   Pharos; Q8IYX7; Tbio.
DR   PRO; PR:Q8IYX7; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8IYX7; protein.
DR   Bgee; ENSG00000155875; Expressed in secondary oocyte and 39 other tissues.
DR   ExpressionAtlas; Q8IYX7; baseline and differential.
DR   Genevisible; Q8IYX7; HS.
DR   GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; IDA:UniProtKB.
DR   GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   InterPro; IPR033336; SAXO1/2.
DR   PANTHER; PTHR31516; PTHR31516; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoskeleton; Flagellum; Reference proteome; Repeat.
FT   CHAIN           1..474
FT                   /note="Stabilizer of axonemal microtubules 1"
FT                   /id="PRO_0000089737"
FT   REGION          30..64
FT                   /note="Mn 1"
FT   REGION          65..97
FT                   /note="Mn 2"
FT   REGION          98..131
FT                   /note="Mn 3"
FT   REGION          132..165
FT                   /note="Mn 4"
FT   REGION          166..199
FT                   /note="Mn 5"
FT   REGION          200..232
FT                   /note="Mn 6"
FT   REGION          233..266
FT                   /note="Mn 7"
FT   REGION          267..299
FT                   /note="Mn 8"
FT   REGION          300..332
FT                   /note="Mn 9"
FT   REGION          333..366
FT                   /note="Mn 10"
FT   REGION          367..400
FT                   /note="Mn 12"
FT   REGION          401..434
FT                   /note="Mn 12"
FT   REGION          446..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         27
FT                   /note="K -> E (in dbSNP:rs7021572)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023229"
FT   VARIANT         63
FT                   /note="P -> S (in dbSNP:rs6475273)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023230"
FT   VARIANT         385
FT                   /note="N -> S (in dbSNP:rs34119945)"
FT                   /id="VAR_057807"
FT   MUTAGEN         116..119
FT                   /note="RVDP->AADA: No effect on subcellular location."
FT                   /evidence="ECO:0000269|PubMed:25673876"
SQ   SEQUENCE   474 AA;  54621 MW;  8D4525BEDE11F5D8 CRC64;
     MKTKCICELC SCGRHHCPHL PTKIYDKTEK PCLLSEYTEN YPFYHSYLPR ESFKPRREYQ
     KGPIPMEGLT TSRRDFGPHK VAPVKVHQYD QFVPSEENMD LLTTYKKDYN PYPVCRVDPI
     KPRDSKYPCS DKMECLPTYK ADYLPWNQPR REPLRLEHKY QPASVRFDNR TTHQDDYPIK
     GLVKTISCKP LAMPKLCNIP LEDVTNYKMS YVAHPVEKRF VHEAEKFRPC EIPFESLTTQ
     KQSYRGLMGE PAKSLKPLAR PPGLDMPFCN TTEFRDKYQA WPMPRMFSKA PITYVPPEDR
     MDLLTTVQAH YTCPKGAPAQ SCRPALQIKK CGRFEGSSTT KDDYKQWSSM RTEPVKPVPQ
     LDLPTEPLDC LTTTRAHYVP HLPINTKSCK PHWSGPRGNV PVESQTTYTI SFTPKEMGRC
     LASYPEPPGY TFEEVDALGH RIYKPVSQAG SQQSSHLSVD DSENPNQREL EVLA
 
 
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