TBCD4_MOUSE
ID TBCD4_MOUSE Reviewed; 1307 AA.
AC Q8BYJ6; Q149C0; Q149C1; Q3T9E8; Q3TAQ5; Q5DU23; Q66JU2; Q6P2M2; Q8BMH6;
AC Q8BXM2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=TBC1 domain family member 4;
DE AltName: Full=Akt substrate of 160 kDa;
DE Short=AS160;
GN Name=Tbc1d4; Synonyms=As160, Kiaa0603;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-840 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Forelimb, Retina, Spinal cord, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-844 (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION AT SER-595 AND THR-649, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11994271; DOI=10.1074/jbc.c200198200;
RA Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
RA Lienhard G.E.;
RT "A method to identify serine kinase substrates. Akt phosphorylates a novel
RT adipocyte protein with a Rab GTPase-activating protein (GAP) domain.";
RL J. Biol. Chem. 277:22115-22118(2002).
RN [5]
RP PHOSPHORYLATION AT SER-324; SER-348; SER-577; SER-595; THR-649 AND SER-758.
RX PubMed=12637568; DOI=10.1074/jbc.c300063200;
RA Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S., Garner C.W.,
RA Lienhard G.E.;
RT "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
RT regulates GLUT4 translocation.";
RL J. Biol. Chem. 278:14599-14602(2003).
RN [6]
RP EFFECT ON GLUT4 TRANSLOCATION.
RX PubMed=15254270; DOI=10.1091/mbc.e04-04-0333;
RA Zeigerer A., McBrayer M.K., McGraw T.E.;
RT "Insulin stimulation of GLUT4 exocytosis, but not its inhibition of
RT endocytosis, is dependent on RabGAP AS160.";
RL Mol. Biol. Cell 15:4406-4415(2004).
RN [7]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=16804075; DOI=10.2337/db06-0175;
RA Treebak J.T., Glund S., Deshmukh A., Klein D.K., Long Y.C., Jensen T.E.,
RA Jorgensen S.B., Viollet B., Andersson L., Neumann D., Wallimann T.,
RA Richter E.A., Chibalin A.V., Zierath J.R., Wojtaszewski J.F.;
RT "AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on
RT AMPK catalytic and regulatory subunits.";
RL Diabetes 55:2051-2058(2006).
RN [8]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=16804077; DOI=10.2337/db06-0150;
RA Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B., Arnolds D.E.,
RA Sakamoto K., Hirshman M.F., Goodyear L.J.;
RT "Distinct signals regulate AS160 phosphorylation in response to insulin,
RT AICAR, and contraction in mouse skeletal muscle.";
RL Diabetes 55:2067-2076(2006).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=18276765; DOI=10.2337/db07-1469;
RA Bouzakri K., Ribaux P., Tomas A., Parnaud G., Rickenbach K., Halban P.A.;
RT "Rab GTPase-activating protein AS160 is a major downstream effector of
RT protein kinase B/Akt signaling in pancreatic beta-cells.";
RL Diabetes 57:1195-1204(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-261; SER-573;
RP SER-577; SER-598; SER-616; THR-620; SER-624; SER-761; SER-764 AND THR-770,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and 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).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-584, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A,
CC RAB10 and RAB14. Promotes insulin-induced glucose transporter
CC SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing
CC glucose uptake (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11994271}.
CC Note=Cytoplasmic perinuclear. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BYJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BYJ6-2; Sequence=VSP_013891, VSP_036876, VSP_036878;
CC Name=3;
CC IsoId=Q8BYJ6-3; Sequence=VSP_036874, VSP_036876, VSP_036878;
CC Name=4;
CC IsoId=Q8BYJ6-4; Sequence=VSP_036873, VSP_013891, VSP_036876,
CC VSP_036878;
CC Name=5;
CC IsoId=Q8BYJ6-5; Sequence=VSP_036872, VSP_036875, VSP_036877;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in pancreatic beta
CC cells. {ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:18276765}.
CC -!- PTM: Phosphorylated by AKT1; insulin-induced. Also phosphorylated by
CC AMPK in response to insulin. Insulin-stimulated phosphorylation is
CC required for SLC2A4/GLUT4 translocation. Has no effect on SLC2A4/GLUT4
CC internalization. {ECO:0000269|PubMed:11994271,
CC ECO:0000269|PubMed:12637568, ECO:0000269|PubMed:16804075,
CC ECO:0000269|PubMed:16804077}.
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DR EMBL; AK039337; BAC30322.2; -; mRNA.
DR EMBL; AK044719; BAC32048.1; -; mRNA.
DR EMBL; AK031120; BAC27263.1; -; mRNA.
DR EMBL; AK171689; BAE42613.1; -; mRNA.
DR EMBL; AK172575; BAE43074.1; -; mRNA.
DR EMBL; BC064433; AAH64433.1; -; mRNA.
DR EMBL; BC080762; AAH80762.1; -; mRNA.
DR EMBL; BC117869; AAI17870.1; -; mRNA.
DR EMBL; BC117870; AAI17871.1; -; mRNA.
DR EMBL; AK220347; BAD90243.1; -; mRNA.
DR RefSeq; NP_001074747.2; NM_001081278.2.
DR RefSeq; XP_006518822.1; XM_006518759.3. [Q8BYJ6-1]
DR RefSeq; XP_011243304.1; XM_011245002.2. [Q8BYJ6-2]
DR AlphaFoldDB; Q8BYJ6; -.
DR SMR; Q8BYJ6; -.
DR BioGRID; 229182; 6.
DR IntAct; Q8BYJ6; 2.
DR MINT; Q8BYJ6; -.
DR STRING; 10090.ENSMUSP00000125509; -.
DR iPTMnet; Q8BYJ6; -.
DR PhosphoSitePlus; Q8BYJ6; -.
DR jPOST; Q8BYJ6; -.
DR MaxQB; Q8BYJ6; -.
DR PaxDb; Q8BYJ6; -.
DR PeptideAtlas; Q8BYJ6; -.
DR PRIDE; Q8BYJ6; -.
DR ProteomicsDB; 254659; -. [Q8BYJ6-1]
DR ProteomicsDB; 254660; -. [Q8BYJ6-2]
DR ProteomicsDB; 254661; -. [Q8BYJ6-3]
DR ProteomicsDB; 254662; -. [Q8BYJ6-4]
DR ProteomicsDB; 254663; -. [Q8BYJ6-5]
DR GeneID; 210789; -.
DR KEGG; mmu:210789; -.
DR UCSC; uc007uvl.1; mouse. [Q8BYJ6-5]
DR UCSC; uc007uvo.2; mouse. [Q8BYJ6-3]
DR UCSC; uc007uvp.2; mouse. [Q8BYJ6-4]
DR UCSC; uc007uvq.2; mouse. [Q8BYJ6-2]
DR UCSC; uc007uvr.2; mouse. [Q8BYJ6-1]
DR CTD; 9882; -.
DR MGI; MGI:2429660; Tbc1d4.
DR eggNOG; KOG4436; Eukaryota.
DR InParanoid; Q8BYJ6; -.
DR OrthoDB; 323342at2759; -.
DR PhylomeDB; Q8BYJ6; -.
DR BioGRID-ORCS; 210789; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tbc1d4; mouse.
DR PRO; PR:Q8BYJ6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BYJ6; protein.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0031339; P:negative regulation of vesicle fusion; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR021785; DUF3350.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF11830; DUF3350; 1.
DR Pfam; PF00640; PID; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; GTPase activation;
KW Methylation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1307
FT /note="TBC1 domain family member 4"
FT /id="PRO_0000208027"
FT DOMAIN 53..209
FT /note="PID 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 319..475
FT /note="PID 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 927..1121
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 324
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:12637568"
FT MOD_RES 348
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:12637568"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 484
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 577
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:12637568,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 584
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 595
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:11994271,
FT ECO:0000269|PubMed:12637568"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 620
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:11994271,
FT ECO:0000269|PubMed:12637568"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60343"
FT MOD_RES 758
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:12637568"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 770
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..793
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036872"
FT VAR_SEQ 508
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036873"
FT VAR_SEQ 685..747
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_013891"
FT VAR_SEQ 685..739
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036874"
FT VAR_SEQ 794..802
FT /note="SPSAMQQQK -> MPLTVFFSA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036875"
FT VAR_SEQ 873
FT /note="E -> G (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_036876"
FT VAR_SEQ 873
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036877"
FT VAR_SEQ 874..1307
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_036878"
FT CONFLICT 171
FT /note="I -> V (in Ref. 1; BAC30322)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="H -> Y (in Ref. 1; BAC30322)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="E -> A (in Ref. 1; BAC30322)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="E -> K (in Ref. 2; AAH64433)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="S -> K (in Ref. 2; AAH80762)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="Q -> L (in Ref. 1; BAE42613)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="R -> K (in Ref. 1; BAE42613)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="A -> T (in Ref. 1; BAE42613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1307 AA; 147451 MW; 60B37CC6ED1D2F55 CRC64;
MESPSCIQDE PFPHPLEPEP SAPAQPGATK PGDKRFRLWY VGGSCLDRRT TLPMLPWLMA
EIRRRSQKPD AGGCGAPAAR EVILVLSAPF LRCVPAPGAG VGGGAGSGAV QPNTGVFIFE
HKAQHISRFI HNSHDLTYFA YLIKAQPDDP ESQMACHVFR ATDPNQVPDV ISSIRQLSKA
AMKEDSKPSK DNEDAFYNSQ KFEVLYCGRV IVTHKKAPSS LIDDCKDKFS LHEQQRLKLQ
GERGGDPGDE MGVLEVESPV SPDDSLPEKA DGTVNSPRAL PSLASLPALA SQPALASSRV
CFPERILEDC GFDEQQEFRS RCSSVTGVMQ KKVHENNQKT QPRRRHASAP SHVQPSDSEK
NRTMLFQVGR FEINLISPDT KSVVLEKNFK DISSCSQGIK HVDHFGFICR ESPEPGLSQY
ICYVFQCANE SLVDEVMLTL KQAFSTAAAL QSAKTQIKLC ETCPMHSLHK LCERIEGLYP
PRAKLVIQRH LSSLTDNEQA DIFERVQKMK PISDQEENEL VILHLRQLCE AKQRTHVHIG
EGPAIISNST IPENVTSGGR FKLDVLKNKA KRSLTSSLEN IFSRGANRMR GRLGSMDSFE
RANSLASEKD FSPGDSPPGT PPASPLSSAW HAFPEEDSDS PQFRRRAHTF SHPPSSSRRK
LNLQDGKAHG LRSPLLRQSS SEQCSIVPSA RRMYKESNSS CSLPSLHTSF SAPSFTAPSF
LKSFYQNSGR LSPQYENEIR QDTASESSDG EGRKRTSSTC SNESLNAGGT PVTPRRVSWR
QRIFLRVASP VNKSPSAMQQ QKDGLDRTEL LPLSPLSPTM EEEPLIIFLS GDEDTEKVEE
KKKSKELKSL WKKAIHQQIL LLRMEKENQK LEEARRDELQ SRKVKLDYEE VGTCQKEILI
AWDKKLLNCR TKIRCDMEDI HTSLKEGVPK SRRGEIWQFL ALQYRLRHRL PNKHQPPDTS
YKELLKQLTA QQHAILVDLG RTFPTHPYFS VQLGAGQLSL FNLLKAYSLL DKEVGYCQGI
SFVAGVLLLH MSEEQAFEML KFLMYDLGFR KQYRPDMMSL QIQMYQLSRL LHDYHRELYN
HLEENEISPS LYAAPWFLTL FASQFPLGFV ARVFDIIFLQ GTEVIFKVAL SLLSSQEALI
MECENFENIV EFLKSTLPDM NTTEMEKIIT QVFEMDISKQ LHAYEVEYHV LQDELLESSY
ACEDNESLEK LERANNQLKR QNMDLLEKLQ VAHAKIQALE SNLETLLTRE TKMKALIRTL
EQDKMAYQKT VEQIRKLLPA DALANCELLL KDLTHPTNDK AKAGNKP
