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 27-MAR-2024, entry version 151. 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; RC 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, RC Spleen, 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}. 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; 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 GlyGen; Q8BYJ6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8BYJ6; -. DR PhosphoSitePlus; Q8BYJ6; -. DR jPOST; Q8BYJ6; -. DR MaxQB; Q8BYJ6; -. DR PaxDb; 10090-ENSMUSP00000125509; -. DR PeptideAtlas; 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 Pumba; Q8BYJ6; -. 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 AGR; MGI:2429660; -. DR CTD; 9882; -. DR MGI; MGI:2429660; Tbc1d4. DR eggNOG; KOG4436; Eukaryota. DR InParanoid; Q8BYJ6; -. DR OrthoDB; 2908929at2759; -. DR PhylomeDB; Q8BYJ6; -. DR BioGRID-ORCS; 210789; 2 hits in 76 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:0032869; P:cellular response to insulin stimulus; IGI:MGI. DR GO; GO:0031339; P:negative regulation of vesicle fusion; ISO:MGI. DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB. DR CDD; cd00934; PTB; 1. DR CDD; cd01269; PTB_TBC1D1_like; 1. DR Gene3D; 1.10.10.2750; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1. DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1. DR InterPro; IPR021785; DUF3350. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR006020; PTB/PI_dom. DR InterPro; IPR000195; Rab-GAP-TBC_dom. DR InterPro; IPR035969; Rab-GAP_TBC_sf. DR PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1. DR PANTHER; PTHR47219:SF13; TBC1 DOMAIN FAMILY MEMBER 4 ISOFORM X1; 1. 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; SSF50729; PH domain-like; 2. DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 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 //