MAGI3_MOUSE
ID MAGI3_MOUSE Reviewed; 1476 AA.
AC Q9EQJ9; B0V3N7; B0V3N8; Q69ZE1; Q8C0P8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3;
DE AltName: Full=Membrane-associated guanylate kinase inverted 3;
DE Short=MAGI-3;
GN Name=Magi3; Synonyms=Kiaa1634;
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 2), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH TGFA.
RX PubMed=15652357; DOI=10.1016/j.yexcr.2004.10.007;
RA Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L.,
RA Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.;
RT "Identification of MAGI-3 as a transforming growth factor-alpha tail
RT binding protein.";
RL Exp. Cell Res. 303:457-470(2005).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-1355 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1476 (ISOFORM 1).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=14645510; DOI=10.1128/mcb.23.24.8970-8981.2003;
RA Nguyen M.M., Nguyen M.L., Caruana G., Bernstein A., Lambert P.F.,
RA Griep A.E.;
RT "Requirement of PDZ-containing proteins for cell cycle regulation and
RT differentiation in the mouse lens epithelium.";
RL Mol. Cell. Biol. 23:8970-8981(2003).
RN [6]
RP INTERACTION WITH DLL1.
RX PubMed=15509766; DOI=10.1242/dev.01417;
RA Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.;
RT "Delta proteins and MAGI proteins: an interaction of Notch ligands with
RT intracellular scaffolding molecules and its significance for zebrafish
RT development.";
RL Development 131:5659-5669(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FZD4; FZD7 AND VANGL2.
RX PubMed=15195140; DOI=10.1038/sj.onc.1207817;
RA Yao R., Natsume Y., Noda T.;
RT "MAGI-3 is involved in the regulation of the JNK signaling pathway as a
RT scaffold protein for frizzled and Ltap.";
RL Oncogene 23:6023-6030(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby
CC regulating various cellular and signaling processes. Cooperates with
CC PTEN to modulate the kinase activity of AKT1. Its interaction with
CC PTPRB and tyrosine phosphorylated proteins suggests that it may link
CC receptor tyrosine phosphatase with its substrates at the plasma
CC membrane. In polarized epithelial cells, involved in efficient
CC trafficking of TGFA to the cell surface. Regulates the ability of LPAR2
CC to activate ERK and RhoA pathways. Regulates the JNK signaling cascade
CC via its interaction with FZD4 and VANGL2. {ECO:0000269|PubMed:15195140,
CC ECO:0000269|PubMed:15652357}.
CC -!- SUBUNIT: Interacts with ADRB1, ADGRB1, LPAR2/EDG4, GRIN2B, PTEN, and
CC PTPRB. Interacts with unidentified tyrosine phosphorylated proteins (By
CC similarity). Interacts with FZD4, FZD7, TGFA and VANGL2. Interacts with
CC DLL1 (PubMed:15509766). Interacts with PRRG4 (via cytoplasmic domain)
CC (By similarity). {ECO:0000250|UniProtKB:Q5TCQ9,
CC ECO:0000250|UniProtKB:Q9JK71, ECO:0000269|PubMed:15195140,
CC ECO:0000269|PubMed:15509766, ECO:0000269|PubMed:15652357}.
CC -!- INTERACTION:
CC Q9EQJ9; P01135: TGFA; Xeno; NbExp=4; IntAct=EBI-7455245, EBI-1034374;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15195140};
CC Peripheral membrane protein {ECO:0000269|PubMed:15195140}. Cell
CC junction, tight junction {ECO:0000269|PubMed:15195140}. Nucleus
CC {ECO:0000250}. Note=Concentrates in specific sites at the plasma
CC membrane and in the nucleus. In epithelial cells, it localizes at tight
CC junctions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQJ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQJ9-2; Sequence=VSP_034288, VSP_034289;
CC -!- TISSUE SPECIFICITY: Widely expressed. Colocalizes with TGFA in neurons
CC in the cortex and dentate gyrus, as well as in ependymal cells and some
CC astrocytes (at protein level). Present in lens epithelium.
CC {ECO:0000269|PubMed:14645510, ECO:0000269|PubMed:15652357}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32503.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AF213258; AAG43836.1; -; mRNA.
DR EMBL; AC162922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK030083; BAC26773.1; -; mRNA.
DR EMBL; AK173225; BAD32503.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS17699.1; -. [Q9EQJ9-2]
DR CCDS; CCDS51031.1; -. [Q9EQJ9-1]
DR RefSeq; NP_598614.1; NM_133853.3. [Q9EQJ9-2]
DR AlphaFoldDB; Q9EQJ9; -.
DR SMR; Q9EQJ9; -.
DR BioGRID; 221259; 2.
DR IntAct; Q9EQJ9; 8.
DR MINT; Q9EQJ9; -.
DR STRING; 10090.ENSMUSP00000112934; -.
DR iPTMnet; Q9EQJ9; -.
DR PhosphoSitePlus; Q9EQJ9; -.
DR jPOST; Q9EQJ9; -.
DR MaxQB; Q9EQJ9; -.
DR PaxDb; Q9EQJ9; -.
DR PeptideAtlas; Q9EQJ9; -.
DR PRIDE; Q9EQJ9; -.
DR ProteomicsDB; 292081; -. [Q9EQJ9-1]
DR ProteomicsDB; 292082; -. [Q9EQJ9-2]
DR Antibodypedia; 1896; 76 antibodies from 22 providers.
DR DNASU; 99470; -.
DR Ensembl; ENSMUST00000064371; ENSMUSP00000067932; ENSMUSG00000052539. [Q9EQJ9-2]
DR Ensembl; ENSMUST00000122303; ENSMUSP00000113713; ENSMUSG00000052539. [Q9EQJ9-2]
DR GeneID; 99470; -.
DR KEGG; mmu:99470; -.
DR UCSC; uc008qua.2; mouse. [Q9EQJ9-2]
DR CTD; 260425; -.
DR MGI; MGI:1923484; Magi3.
DR VEuPathDB; HostDB:ENSMUSG00000052539; -.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000156496; -.
DR HOGENOM; CLU_004562_1_0_1; -.
DR InParanoid; Q9EQJ9; -.
DR OMA; ASYRHSW; -.
DR PhylomeDB; Q9EQJ9; -.
DR BioGRID-ORCS; 99470; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Magi3; mouse.
DR PRO; PR:Q9EQJ9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9EQJ9; protein.
DR Bgee; ENSMUSG00000052539; Expressed in atrioventricular valve and 235 other tissues.
DR ExpressionAtlas; Q9EQJ9; baseline and differential.
DR Genevisible; Q9EQJ9; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005109; F:frizzled binding; IPI:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IGI:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030035; MAGI3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF10; PTHR10316:SF10; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell junction; Cell membrane; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Tight junction.
FT CHAIN 1..1476
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 3"
FT /id="PRO_0000341408"
FT DOMAIN 18..108
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 116..290
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 296..329
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 342..375
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 413..495
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 581..657
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 729..811
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 852..939
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1022..1104
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 18..108
FT /note="Interaction with ADRB1 and TGFA"
FT /evidence="ECO:0000269|PubMed:15652357"
FT REGION 184..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..495
FT /note="Interaction with PTEN"
FT /evidence="ECO:0000250"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..811
FT /note="Interaction with ADGRB1"
FT /evidence="ECO:0000250"
FT REGION 818..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..939
FT /note="Interaction with LPAR2 and GRIN2B"
FT /evidence="ECO:0000250"
FT REGION 939..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TCQ9"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK71"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TCQ9"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK71"
FT VAR_SEQ 1112..1126
FT /note="DWDTNSPSSSNVIYD -> LAPSGLCSYVKPEQH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15652357,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034288"
FT VAR_SEQ 1127..1476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15652357,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034289"
FT CONFLICT 625
FT /note="I -> N (in Ref. 3; BAC26773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1476 AA; 161672 MW; A9F041B5EA4B6F3F CRC64;
MSKTLKKKKH WLSKVQECAV SWAGPPGDLG AEIRGGAERG EFPYLGRLRD EAGGGGGTCC
VVSGKAPSPG DVLLEVNGTP VSGLTNRDTL AVIRHFREPI RLKTVKPGKV INKDLRHYLS
LQFQKGSIDH KLQQVIRDNL YLRTIPCTTR APRDGEVPGV DYNFISVEQF KALEESGALL
ESGTYDGNFY GTPKPPAEPS PFQPDPVDQV LFDNEFDTES QRKRTTSVSK MERMDSSLPE
EEEDEDKEAV NGSGSMETRE MHSETSDCWM KTVPSYNQTN SSMDFRNYMM RDENLEPLPK
NWEMAYTDTG MIYFIDHNTK TTTWLDPRLC KKAKAPEDCE DGELPYGWEK IEDPQYGTYY
VDHLNQKTQF ENPVEEAKRK KQLGQAEIHS AKTDVERAHF TRDPSQLKGV LVRASLKKST
MGFGFTIIGG DRPDEFLQVK NVLKDGPAAQ DGKIAPGDVI VDINGNCVLG HTHADVVQMF
QLVPVNQYVN LTLCRGYPLP DDSEDPVVDI VAATPVINGQ SLTKGETCMN TQDFKLGAMV
LDQNGKSGQI LASDRLNGPS ESSEQRASLA SSGSSQPELV TIPLIKGPKG FGFAIADSPT
GQKVKMILDS QWCQGLQKGD IIKEIYHQNV QNLTHLQVVE VLKQFPVGAD VPLLILRGGP
CSPTKTAKTK TDTKENSGSL ETINEPIPQP MPFPPSIIRS GSPKLDPSEV YLKSKTLYED
KPPNTKDLDV FLRKQESGFG FRVLGGDGPD QSIYIGAIIP LGAAEKDGRL RAADELMCID
GIPVKGKSHK QVLDLMTTAA RNGHVLLTVR RKIFYGEKQP EDESHQAFSQ NGSPRLNRAE
LPTRSAPQEA YDVTLQRKEN EGFGFVILTS KSKPPPGVIP HKIGRVIDGS PADRCGGLKV
GDHISAVNGQ SIVDLSHDNI VQLIKDAGVT VTLTVVAEEE HHGPPSGTNS ARQSPALQHR
PMGQAQANHI PGDRIALEGE IGRDVCSSYR HSWSDHKHLA QPDTAVISVV GSRHNQSLGC
YPVELERGPR GFGFSLRGGK EYNMGLFILR LAEDGPAIKD GRIHVGDQIV EINGEPTQGI
THTRAIELIQ AGGNKVLLLL RPGTGLIPDH GDWDTNSPSS SNVIYDEQPP PLPSSHSAST
FEESHVPATE DSLTRVQICE KAEELKDTVQ EKKSTLNGSQ PEMKYQSVHK TMSKKDPPRG
SGHGEKSRLK GENGVTRRGR SASPKKSVNR HSEEHLEKIP RPLKSDPKEK SRDRSLSPRK
GESKGRLTIK AGSGQDPYRK DRGRSSSPKK QQKIGGNSLS NTEGKLSEAG SRRAAGHPRD
STEQLPDGRE KSGVSRKDLK QSQPGKTRTK SPEKKSSKVD ETSLPSKKTS STAGRVVSEK
EKGKKPTAGE TSRETVEHTQ ISAKQLKQEA QEKTALGNAD DHKGRESEVT DRCRERAGCT
PQSSSLVKKA PITPGPWRVP RANKVTGTTG MADKQL
