AGAP3_HUMAN
ID AGAP3_HUMAN Reviewed; 875 AA.
AC Q96P47; B3KNZ8; E9PAL8; Q59EN0; Q96RK3;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3;
DE Short=AGAP-3;
DE AltName: Full=CRAM-associated GTPase;
DE Short=CRAG;
DE AltName: Full=Centaurin-gamma-3;
DE Short=Cnt-g3;
DE AltName: Full=MR1-interacting protein;
DE Short=MRIP-1;
GN Name=AGAP3; Synonyms=CENTG3;
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).
RC TISSUE=Heart;
RX PubMed=12640130; DOI=10.1128/mcb.23.7.2476-2488.2003;
RA Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.;
RT "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating
RT proteins.";
RL Mol. Cell. Biol. 23:2476-2488(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hong W.;
RT "MRIP-1 as a member (centaurin gamma3) of the centaurin ArfGAP protein
RT family.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-855 (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15381706; DOI=10.1074/jbc.m410565200;
RA Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT cyclase.";
RL J. Biol. Chem. 279:49346-49354(2004).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PML, ACTIVITY
RP REGULATION, AND FUNCTION.
RX PubMed=16461359; DOI=10.1083/jcb.200505079;
RA Qin Q., Inatome R., Hotta A., Kojima M., Yamamura H., Hirai H.,
RA Yoshizawa T., Tanaka H., Fukami K., Yanagi S.;
RT "A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated
RT nuclear body formation and degradation of expanded polyglutamine protein.";
RL J. Cell Biol. 172:497-504(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324 AND THR-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324; SER-443 AND SER-538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 90-255.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the Ras-like domain of CENTG3.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family (Potential). GTPase which may be involved in the degradation of
CC expanded polyglutamine proteins through the ubiquitin-proteasome
CC pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}.
CC -!- ACTIVITY REGULATION: GTPase activity is stimulated by oxidative stress.
CC {ECO:0000269|PubMed:16461359}.
CC -!- SUBUNIT: Interacts with PML. Interacts with expanded polyglutamine
CC proteins. {ECO:0000269|PubMed:16461359}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16461359}. Note=In
CC cells upon oxidative stress or in brains of Machado-Joseph disease
CC patients, translocates to PML nuclear bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96P47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96P47-2; Sequence=VSP_018534, VSP_018535;
CC Name=3;
CC IsoId=Q96P47-3; Sequence=VSP_018536, VSP_018537;
CC Name=4;
CC IsoId=Q96P47-4; Sequence=VSP_040373;
CC Name=5;
CC IsoId=Q96P47-5; Sequence=VSP_054890, VSP_054891;
CC Name=6;
CC IsoId=Q96P47-6; Sequence=VSP_040373, VSP_018536, VSP_018537;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15381706,
CC ECO:0000269|PubMed:16461359}.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
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DR EMBL; AF359283; AAK48932.2; -; mRNA.
DR EMBL; AF413079; AAL04173.1; -; mRNA.
DR EMBL; AK055393; BAG51510.1; -; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471173; EAW54026.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54028.1; -; Genomic_DNA.
DR EMBL; AB209781; BAD93018.1; -; mRNA.
DR CCDS; CCDS43681.1; -. [Q96P47-4]
DR CCDS; CCDS55185.1; -. [Q96P47-6]
DR CCDS; CCDS64802.1; -. [Q96P47-5]
DR RefSeq; NP_001036000.1; NM_001042535.3. [Q96P47-6]
DR RefSeq; NP_001268229.1; NM_001281300.1. [Q96P47-5]
DR RefSeq; NP_114152.3; NM_031946.6. [Q96P47-4]
DR RefSeq; XP_016867223.1; XM_017011734.1.
DR PDB; 3IHW; X-ray; 1.92 A; A=90-255.
DR PDBsum; 3IHW; -.
DR AlphaFoldDB; Q96P47; -.
DR SMR; Q96P47; -.
DR BioGRID; 125551; 78.
DR IntAct; Q96P47; 22.
DR MINT; Q96P47; -.
DR STRING; 9606.ENSP00000380413; -.
DR iPTMnet; Q96P47; -.
DR PhosphoSitePlus; Q96P47; -.
DR BioMuta; AGAP3; -.
DR DMDM; 97535922; -.
DR EPD; Q96P47; -.
DR jPOST; Q96P47; -.
DR MassIVE; Q96P47; -.
DR MaxQB; Q96P47; -.
DR PaxDb; Q96P47; -.
DR PeptideAtlas; Q96P47; -.
DR PRIDE; Q96P47; -.
DR ProteomicsDB; 19042; -.
DR ProteomicsDB; 3514; -.
DR ProteomicsDB; 77618; -. [Q96P47-1]
DR ProteomicsDB; 77619; -. [Q96P47-2]
DR ProteomicsDB; 77620; -. [Q96P47-3]
DR ProteomicsDB; 77621; -. [Q96P47-4]
DR Antibodypedia; 1445; 154 antibodies from 28 providers.
DR DNASU; 116988; -.
DR Ensembl; ENST00000397238.7; ENSP00000380413.2; ENSG00000133612.19. [Q96P47-4]
DR Ensembl; ENST00000463381.5; ENSP00000418016.1; ENSG00000133612.19. [Q96P47-5]
DR Ensembl; ENST00000473312.5; ENSP00000418921.1; ENSG00000133612.19. [Q96P47-6]
DR Ensembl; ENST00000622464.4; ENSP00000480655.1; ENSG00000133612.19. [Q96P47-1]
DR GeneID; 116988; -.
DR KEGG; hsa:116988; -.
DR MANE-Select; ENST00000397238.7; ENSP00000380413.2; NM_031946.7; NP_114152.3. [Q96P47-4]
DR UCSC; uc003wje.3; human. [Q96P47-1]
DR CTD; 116988; -.
DR DisGeNET; 116988; -.
DR GeneCards; AGAP3; -.
DR HGNC; HGNC:16923; AGAP3.
DR HPA; ENSG00000133612; Low tissue specificity.
DR neXtProt; NX_Q96P47; -.
DR OpenTargets; ENSG00000133612; -.
DR PharmGKB; PA26413; -.
DR VEuPathDB; HostDB:ENSG00000133612; -.
DR eggNOG; KOG0705; Eukaryota.
DR GeneTree; ENSGT00940000159586; -.
DR HOGENOM; CLU_007326_4_0_1; -.
DR InParanoid; Q96P47; -.
DR OMA; NMSEVPK; -.
DR PhylomeDB; Q96P47; -.
DR TreeFam; TF317762; -.
DR PathwayCommons; Q96P47; -.
DR SignaLink; Q96P47; -.
DR BioGRID-ORCS; 116988; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; AGAP3; human.
DR EvolutionaryTrace; Q96P47; -.
DR GeneWiki; CENTG3; -.
DR GenomeRNAi; 116988; -.
DR Pharos; Q96P47; Tbio.
DR PRO; PR:Q96P47; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96P47; protein.
DR Bgee; ENSG00000133612; Expressed in right hemisphere of cerebellum and 178 other tissues.
DR ExpressionAtlas; Q96P47; baseline and differential.
DR Genevisible; Q96P47; HS.
DR GO; GO:0071944; C:cell periphery; ISO:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:UniProtKB.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cytoplasm; GTP-binding;
KW GTPase activation; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..875
FT /note="Arf-GAP with GTPase, ANK repeat and PH domain-
FT containing protein 3"
FT /id="PRO_0000074220"
FT DOMAIN 367..605
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 626..746
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 748..777
FT /note="ANK 1"
FT REPEAT 785..814
FT /note="ANK 2"
FT REPEAT 818..847
FT /note="ANK 3"
FT ZN_FING 641..664
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..375
FT /note="Small GTPase-like"
FT REGION 428..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 142..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 198..201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..192
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054890"
FT VAR_SEQ 1..4
FT /note="MNFQ -> MFGGAGPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018534"
FT VAR_SEQ 9..15
FT /note="QSPQQQQ -> GPSQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018535"
FT VAR_SEQ 15
FT /note="Q -> QSLAAPGGGGAAAQQLVCGGQFGGAGPGAGGGGGPSQ (in
FT isoform 4 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_040373"
FT VAR_SEQ 341..360
FT /note="SRKGADLDREKKAAECKVDS -> ICATVSNFSSTKRPFQLLPN (in
FT isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_018536"
FT VAR_SEQ 361..875
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_018537"
FT VAR_SEQ 463..565
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054891"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3IHW"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3IHW"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3IHW"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:3IHW"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:3IHW"
SQ SEQUENCE 875 AA; 95044 MW; 3F0D04EE00F42E1E CRC64;
MNFQAGGGQS PQQQQQLAGG PPQQFALSNS AAIRAEIQRF ESVHPNIYAI YDLIERIEDL
ALQNQIREHV ISIEDSFVNS QEWTLSRSVP ELKVGIVGNL SSGKSALVHR YLTGTYVQEE
SPEGGRFKKE IVVDGQSYLL LIRDEGGPPE LQFAAWVDAV VFVFSLEDEI SFQTVYNYFL
RLCSFRNASE VPMVLVGTQD AISAANPRVI DDSRARKLST DLKRCTYYET CATYGLNVER
VFQDVAQKVV ALRKKQQLAI GPCKSLPNSP SHSAVSAASI PAVHINQATN GGGSAFSDYS
SSVPSTPSIS QRELRIETIA ASSTPTPIRK QSKRRSNIFT SRKGADLDRE KKAAECKVDS
IGSGRAIPIK QGILLKRSGK SLNKEWKKKY VTLCDNGLLT YHPSLHDYMQ NIHGKEIDLL
RTTVKVPGKR LPRATPATAP GTSPRANGLS VERSNTQLGG GTGAPHSASS ASLHSERPLS
SSAWAGPRPE GLHQRSCSVS SADQWSEATT SLPPGMQHPA SGPAEVLSSS PKLDPPPSPH
SNRKKHRRKK STGTPRPDGP SSATEEAEES FEFVVVSLTG QTWHFEASTA EERELWVQSV
QAQILASLQG CRSAKDKTRL GNQNAALAVQ AVRTVRGNSF CIDCDAPNPD WASLNLGALM
CIECSGIHRH LGAHLSRVRS LDLDDWPPEL LAVMTAMGNA LANSVWEGAL GGYSKPGPDA
CREEKERWIR AKYEQKLFLA PLPSSDVPLG QQLLRAVVED DLRLLVMLLA HGSKEEVNET
YGDGDGRTAL HLSSAMANVV FTQLLIWYGV DVRSRDARGL TPLAYARRAG SQECADILIQ
HGCPGEGCGL APTPNREPAN GTNPSAELHR SPSLL
