位置:首页 > 蛋白库 > ST4A1_HUMAN
ST4A1_HUMAN
ID   ST4A1_HUMAN             Reviewed;         284 AA.
AC   Q9BR01; B2R7N3; O43728;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Sulfotransferase 4A1;
DE            Short=ST4A1;
DE            EC=2.8.2.-;
DE   AltName: Full=Brain sulfotransferase-like protein;
DE            Short=hBR-STL;
DE            Short=hBR-STL-1;
DE   AltName: Full=Nervous system sulfotransferase;
DE            Short=NST;
GN   Name=SULT4A1; Synonyms=SULTX3;
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), AND CHARACTERIZATION.
RC   TISSUE=Brain;
RX   PubMed=10698717; DOI=10.1042/bj3460857;
RA   Falany C.N., Xie X., Wang J., Ferrer J., Falany J.L.;
RT   "Molecular cloning and expression of novel sulphotransferase-like cDNAs
RT   from human and rat brain.";
RL   Biochem. J. 346:857-864(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC   TISSUE=Brain;
RX   PubMed=12039030; DOI=10.1016/s0378-1119(02)00431-6;
RA   Sakakibara Y., Suiko M., Pai T.G., Nakayama T., Takami Y., Katafuchi J.,
RA   Liu M.-C.;
RT   "Highly conserved mouse and human brain sulfotransferases: molecular
RT   cloning, expression, and functional characterization.";
RL   Gene 285:39-47(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   TISSUE=Brain;
RA   Martin S.C., Farb D.H.;
RT   "Molecular identification of a human nervous system cytoplasmic
RT   sulfotransferase, NST.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   TISSUE=Brain;
RA   Walther S.E., Raftogianis R.B.;
RT   "Molecular and physical characterization of human SULT4A1, representing a
RT   novel cytosolic sulfotransferase 1 family.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=12529303; DOI=10.1101/gr.695703;
RA   Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA   Bye J.M., Beare D.M., Dunham I.;
RT   "Reevaluating human gene annotation: a second-generation analysis of
RT   chromosome 22.";
RL   Genome Res. 13:27-36(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Fetal brain, Hippocampus, and Hypothalamus;
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS), FUNCTION, AND CHARACTERIZATION.
RX   PubMed=17425406; DOI=10.1371/journal.pbio.0050097;
RA   Allali-Hassani A., Pan P.W., Dombrovski L., Najmanovich R., Tempel W.,
RA   Dong A., Loppnau P., Martin F., Thornton J., Edwards A.M., Bochkarev A.,
RA   Plotnikov A.N., Vedadi M., Arrowsmith C.H.;
RT   "Structural and chemical profiling of the human cytosolic
RT   sulfotransferases.";
RL   PLoS Biol. 5:E97-E97(2007).
CC   -!- FUNCTION: Atypical sulfotransferase family member with very low
CC       affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low
CC       catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-
CC       nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in
CC       the metabolism of drugs and neurotransmitters in the CNS.
CC       {ECO:0000269|PubMed:17425406}.
CC   -!- INTERACTION:
CC       Q9BR01; Q9UPT6: MAPK8IP3; NbExp=3; IntAct=EBI-6690555, EBI-717887;
CC       Q9BR01; Q13526: PIN1; NbExp=4; IntAct=EBI-6690555, EBI-714158;
CC       Q9BR01; Q9NUX5: POT1; NbExp=2; IntAct=EBI-6690555, EBI-752420;
CC       Q9BR01; Q9BR01: SULT4A1; NbExp=6; IntAct=EBI-6690555, EBI-6690555;
CC       Q9BR01; P22735: TGM1; NbExp=3; IntAct=EBI-6690555, EBI-2562368;
CC       Q9BR01-2; Q92870-2: APBB2; NbExp=3; IntAct=EBI-25831443, EBI-21535880;
CC       Q9BR01-2; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-25831443, EBI-702390;
CC       Q9BR01-2; P14136: GFAP; NbExp=3; IntAct=EBI-25831443, EBI-744302;
CC       Q9BR01-2; P42858: HTT; NbExp=15; IntAct=EBI-25831443, EBI-466029;
CC       Q9BR01-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25831443, EBI-1055254;
CC       Q9BR01-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-25831443, EBI-713665;
CC       Q9BR01-2; P29474: NOS3; NbExp=3; IntAct=EBI-25831443, EBI-1391623;
CC       Q9BR01-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25831443, EBI-25882629;
CC       Q9BR01-2; P37840: SNCA; NbExp=3; IntAct=EBI-25831443, EBI-985879;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BR01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BR01-2; Sequence=VSP_006304;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the cerebral cortex and frontal
CC       lobe, slightly less in the cerebellum, occipital and temporal lobes,
CC       relatively low in the medulla and putamen, and lowest in the spinal
CC       cord. No expression detected in the pancreas (PubMed:10698717). Highly
CC       expressed in fetal brain and occipital lobe, slightly less in the whole
CC       brain, frontal lobe, hippocampus, and lung, very low expression in
CC       cerebellum, medulla oblongata, temporal lobe, testis, kidney and
CC       appendix (PubMed:12039030). {ECO:0000269|PubMed:10698717,
CC       ECO:0000269|PubMed:12039030}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF188698; AAF61197.1; -; mRNA.
DR   EMBL; AF115311; AAF21970.1; -; mRNA.
DR   EMBL; AF176342; AAK64595.1; -; mRNA.
DR   EMBL; AF251263; AAF98152.1; -; mRNA.
DR   EMBL; AL590119; CAC34872.1; -; mRNA.
DR   EMBL; CR456588; CAG30474.1; -; mRNA.
DR   EMBL; AK313048; BAG35880.1; -; mRNA.
DR   EMBL; Z97055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471138; EAW73320.1; -; Genomic_DNA.
DR   EMBL; BC022459; AAH22459.1; -; mRNA.
DR   EMBL; BC028171; AAH28171.1; -; mRNA.
DR   EMBL; BC030665; AAH30665.1; -; mRNA.
DR   CCDS; CCDS14051.1; -. [Q9BR01-1]
DR   RefSeq; NP_055166.1; NM_014351.3. [Q9BR01-1]
DR   PDB; 1ZD1; X-ray; 2.24 A; A/B=1-284.
DR   PDBsum; 1ZD1; -.
DR   AlphaFoldDB; Q9BR01; -.
DR   SMR; Q9BR01; -.
DR   BioGRID; 117358; 21.
DR   IntAct; Q9BR01; 19.
DR   MINT; Q9BR01; -.
DR   STRING; 9606.ENSP00000332565; -.
DR   ChEMBL; CHEMBL1743298; -.
DR   DrugBank; DB12471; Ibrexafungerp.
DR   DrugBank; DB00968; Methyldopa.
DR   DrugBank; DB00960; Pindolol.
DR   DrugBank; DB00871; Terbutaline.
DR   iPTMnet; Q9BR01; -.
DR   PhosphoSitePlus; Q9BR01; -.
DR   BioMuta; SULT4A1; -.
DR   DMDM; 22096149; -.
DR   MassIVE; Q9BR01; -.
DR   PaxDb; Q9BR01; -.
DR   PeptideAtlas; Q9BR01; -.
DR   PRIDE; Q9BR01; -.
DR   ProteomicsDB; 78733; -. [Q9BR01-1]
DR   ProteomicsDB; 78734; -. [Q9BR01-2]
DR   Antibodypedia; 304; 172 antibodies from 26 providers.
DR   DNASU; 25830; -.
DR   Ensembl; ENST00000330884.9; ENSP00000332565.4; ENSG00000130540.14. [Q9BR01-1]
DR   Ensembl; ENST00000422525.1; ENSP00000388285.1; ENSG00000130540.14. [Q9BR01-2]
DR   GeneID; 25830; -.
DR   KEGG; hsa:25830; -.
DR   MANE-Select; ENST00000330884.9; ENSP00000332565.4; NM_014351.4; NP_055166.1.
DR   UCSC; uc003bee.2; human. [Q9BR01-1]
DR   CTD; 25830; -.
DR   DisGeNET; 25830; -.
DR   GeneCards; SULT4A1; -.
DR   HGNC; HGNC:14903; SULT4A1.
DR   HPA; ENSG00000130540; Tissue enriched (brain).
DR   MIM; 608359; gene.
DR   neXtProt; NX_Q9BR01; -.
DR   OpenTargets; ENSG00000130540; -.
DR   PharmGKB; PA412; -.
DR   VEuPathDB; HostDB:ENSG00000130540; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000158662; -.
DR   HOGENOM; CLU_027239_1_1_1; -.
DR   InParanoid; Q9BR01; -.
DR   OMA; MVESCHQ; -.
DR   OrthoDB; 780670at2759; -.
DR   PhylomeDB; Q9BR01; -.
DR   TreeFam; TF321745; -.
DR   BRENDA; 2.8.2.1; 2681.
DR   PathwayCommons; Q9BR01; -.
DR   Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR   SignaLink; Q9BR01; -.
DR   SIGNOR; Q9BR01; -.
DR   BioGRID-ORCS; 25830; 8 hits in 1067 CRISPR screens.
DR   EvolutionaryTrace; Q9BR01; -.
DR   GeneWiki; SULT4A1; -.
DR   GenomeRNAi; 25830; -.
DR   Pharos; Q9BR01; Tbio.
DR   PRO; PR:Q9BR01; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9BR01; protein.
DR   Bgee; ENSG00000130540; Expressed in right frontal lobe and 138 other tissues.
DR   ExpressionAtlas; Q9BR01; baseline and differential.
DR   Genevisible; Q9BR01; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0140059; P:dendrite arborization; IEA:Ensembl.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Lipid metabolism;
KW   Phosphoprotein; Reference proteome; Steroid metabolism; Transferase.
FT   CHAIN           1..284
FT                   /note="Sulfotransferase 4A1"
FT                   /id="PRO_0000085167"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P63047"
FT   MOD_RES         11
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P63047"
FT   MOD_RES         205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         248..284
FT                   /note="GRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL -> AHCVFARKIFL
FT                   SW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12529303,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006304"
FT   CONFLICT        55..56
FT                   /note="KS -> P (in Ref. 10; AAH30665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="N -> S (in Ref. 10; AAH22459)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           35..39
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           59..68
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           96..101
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           135..144
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           158..166
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           175..183
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   TURN            184..187
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           203..213
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           220..235
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:1ZD1"
FT   HELIX           259..273
FT                   /evidence="ECO:0007829|PDB:1ZD1"
SQ   SEQUENCE   284 AA;  33085 MW;  A6EA6844B66C400B CRC64;
     MAESEAETPS TPGEFESKYF EFHGVRLPPF CRGKMEEIAN FPVRPSDVWI VTYPKSGTSL
     LQEVVYLVSQ GADPDEIGLM NIDEQLPVLE YPQPGLDIIK ELTSPRLIKS HLPYRFLPSD
     LHNGDSKVIY MARNPKDLVV SYYQFHRSLR TMSYRGTFQE FCRRFMNDKL GYGSWFEHVQ
     EFWEHRMDSN VLFLKYEDMH RDLVTMVEQL ARFLGVSCDK AQLEALTEHC HQLVDQCCNA
     EALPVGRGRV GLWKDIFTVS MNEKFDLVYK QKMGKCDLTF DFYL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024