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GTPase-activating protein and VPS9 domain-containing protein 1 (GAPex-5) (Rab5-activating protein 6)

 GAPD1_MOUSE             Reviewed;        1458 AA.
Q6PAR5; A0PJI8; A2AR09; A2AR10; A2AR17; A2AR18; Q3TNS1; Q3UDL0;
Q3UYD5; Q6ZPP0; Q80V37; Q80ZK4; Q8BTS5; Q9CRS2; Q9CTI1;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
18-JUL-2018, entry version 115.
RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
AltName: Full=GAPex-5;
AltName: Full=Rab5-activating protein 6;
Name=Gapvd1; Synonyms=Gapex5, Kiaa1521;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TRIP10.
STRAIN=Swiss albino;
PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T.,
Inoue M., Pessin J.E., Saltiel A.R.;
"Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates
Glut4 trafficking in adipocytes.";
Cell Metab. 5:59-72(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1458 (ISOFORM 6).
STRAIN=C57BL/6J, and NOD;
TISSUE=Eye, Liver, Medulla oblongata, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
TISSUE=Brain, Kidney, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=16880210; DOI=10.1074/jbc.M602873200;
Su X., Lodhi I.J., Saltiel A.R., Stahl P.D.;
"Insulin-stimulated Interaction between insulin receptor substrate 1
and p85alpha and activation of protein kinase B/Akt require Rab5.";
J. Biol. Chem. 281:27982-27990(2006).
[7]
FUNCTION.
PubMed=17545148; DOI=10.1074/jbc.M703725200;
Su X., Kong C., Stahl P.D.;
"GAPex-5 mediates ubiquitination, trafficking, and degradation of
epidermal growth factor receptor.";
J. Biol. Chem. 282:21278-21284(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566; SER-569; SER-742;
SER-757; SER-902; SER-908 AND SER-1044, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a
guanine nucleotide exchange factor (GEF), and participates in
various processes such as endocytosis, insulin receptor
internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the
Ras-related protein RAB31 by exchanging bound GDP for free GTP,
leading to regulate LC2A4/GLUT4 trafficking. In the absence of
insulin, it maintains RAB31 in an active state and promotes a
futile cycle between LC2A4/GLUT4 storage vesicles and early
endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin
stimulation, it is translocated to the plasma membrane, releasing
LC2A4/GLUT4 from intracellular storage vesicles. Also involved in
EGFR trafficking and degradation, possibly by promoting EGFR
ubiquitination and subsequent degradation by the proteasome. Has
GEF activity for Rab5 and GAP activity for Ras.
{ECO:0000269|PubMed:16880210, ECO:0000269|PubMed:17189207,
ECO:0000269|PubMed:17545148}.
-!- SUBUNIT: Interacts with RAB5A (By similarity). Interacts with
TRIP10/CIP4. {ECO:0000250, ECO:0000269|PubMed:17189207}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17189207};
Peripheral membrane protein {ECO:0000269|PubMed:17189207}.
Endosome {ECO:0000250}. Note=Recruited to the plasma membrane by
TRIP10/CIP4 in response to insulin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q6PAR5-1; Sequence=Displayed;
Name=2;
IsoId=Q6PAR5-2; Sequence=VSP_032366;
Name=3;
IsoId=Q6PAR5-3; Sequence=VSP_032363, VSP_032364;
Name=4;
IsoId=Q6PAR5-4; Sequence=VSP_032365, VSP_032366;
Name=5;
IsoId=Q6PAR5-5; Sequence=VSP_032366, VSP_032368;
Name=6;
IsoId=Q6PAR5-6; Sequence=VSP_032367;
-!- TISSUE SPECIFICITY: Present in adipocytes and fibroblasts (at
protein level). Ubiquitously expressed.
{ECO:0000269|PubMed:17189207}.
-!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH31478.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH43715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH48847.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH57164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB29377.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC98191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE22277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE29251.1; Type=Frameshift; Positions=811; Evidence={ECO:0000305};
Sequence=CAM15445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM15446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM15455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM15456.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM24604.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM24605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; EF155419; ABM68541.1; -; mRNA.
EMBL; AK129381; BAC98191.1; ALT_INIT; Transcribed_RNA.
EMBL; AK014474; BAB29377.2; ALT_INIT; mRNA.
EMBL; AK088851; BAC40613.1; -; mRNA.
EMBL; AK003521; BAB22834.1; -; mRNA.
EMBL; AK134776; BAE22277.1; ALT_INIT; mRNA.
EMBL; AK150026; BAE29251.1; ALT_FRAME; mRNA.
EMBL; AK165047; BAE38017.1; -; mRNA.
EMBL; AL845262; CAM15445.1; ALT_SEQ; Genomic_DNA.
EMBL; AL929106; CAM15445.1; JOINED; Genomic_DNA.
EMBL; AL845262; CAM15446.1; ALT_SEQ; Genomic_DNA.
EMBL; AL929106; CAM15446.1; JOINED; Genomic_DNA.
EMBL; AL845262; CAM15447.1; -; Genomic_DNA.
EMBL; AL929106; CAM15447.1; JOINED; Genomic_DNA.
EMBL; AL845262; CAM15455.1; ALT_SEQ; Genomic_DNA.
EMBL; AL845262; CAM15456.1; ALT_SEQ; Genomic_DNA.
EMBL; AL929106; CAM24604.1; ALT_SEQ; Genomic_DNA.
EMBL; AL845262; CAM24604.1; JOINED; Genomic_DNA.
EMBL; AL929106; CAM24605.1; ALT_SEQ; Genomic_DNA.
EMBL; AL845262; CAM24605.1; JOINED; Genomic_DNA.
EMBL; AL929106; CAM24606.1; -; Genomic_DNA.
EMBL; AL845262; CAM24606.1; JOINED; Genomic_DNA.
EMBL; BC031478; AAH31478.1; ALT_SEQ; mRNA.
EMBL; BC043715; AAH43715.1; ALT_INIT; mRNA.
EMBL; BC048847; AAH48847.1; ALT_SEQ; mRNA.
EMBL; BC057164; AAH57164.1; ALT_INIT; mRNA.
EMBL; BC060123; AAH60123.1; -; mRNA.
CCDS; CCDS15949.1; -. [Q6PAR5-2]
RefSeq; NP_079985.2; NM_025709.2. [Q6PAR5-2]
RefSeq; XP_011237449.1; XM_011239147.1. [Q6PAR5-4]
RefSeq; XP_011237450.1; XM_011239148.2.
UniGene; Mm.156452; -.
UniGene; Mm.393397; -.
ProteinModelPortal; Q6PAR5; -.
SMR; Q6PAR5; -.
BioGrid; 211649; 1.
IntAct; Q6PAR5; 3.
MINT; Q6PAR5; -.
STRING; 10090.ENSMUSP00000028224; -.
iPTMnet; Q6PAR5; -.
PhosphoSitePlus; Q6PAR5; -.
PaxDb; Q6PAR5; -.
PeptideAtlas; Q6PAR5; -.
PRIDE; Q6PAR5; -.
Ensembl; ENSMUST00000028224; ENSMUSP00000028224; ENSMUSG00000026867. [Q6PAR5-2]
Ensembl; ENSMUST00000102800; ENSMUSP00000099864; ENSMUSG00000026867. [Q6PAR5-2]
Ensembl; ENSMUST00000113099; ENSMUSP00000108723; ENSMUSG00000026867. [Q6PAR5-1]
GeneID; 66691; -.
KEGG; mmu:66691; -.
UCSC; uc008jiq.2; mouse. [Q6PAR5-2]
UCSC; uc008jir.1; mouse. [Q6PAR5-3]
UCSC; uc012bug.1; mouse. [Q6PAR5-4]
CTD; 26130; -.
MGI; MGI:1913941; Gapvd1.
eggNOG; ENOG410IQ83; Eukaryota.
eggNOG; ENOG410XRXX; LUCA.
GeneTree; ENSGT00530000063341; -.
HOVERGEN; HBG107936; -.
InParanoid; Q6PAR5; -.
OMA; MEAFKQR; -.
OrthoDB; EOG091G00G1; -.
PhylomeDB; Q6PAR5; -.
TreeFam; TF105908; -.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
PRO; PR:Q6PAR5; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026867; -.
CleanEx; MM_GAPVD1; -.
ExpressionAtlas; Q6PAR5; baseline and differential.
Genevisible; Q6PAR5; MM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0032794; F:GTPase activating protein binding; IMP:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.20.1050.80; -; 1.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
Pfam; PF00616; RasGAP; 1.
Pfam; PF02204; VPS9; 1.
SMART; SM00167; VPS9; 1.
SUPFAM; SSF109993; SSF109993; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PROSITE; PS51205; VPS9; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endocytosis; Endosome;
GTPase activation; Guanine-nucleotide releasing factor; Membrane;
Phosphoprotein; Reference proteome.
CHAIN 1 1458 GTPase-activating protein and VPS9
domain-containing protein 1.
/FTId=PRO_0000324772.
DOMAIN 131 353 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
DOMAIN 1318 1458 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 390 390 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 458 458 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 470 470 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 762 762 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 902 902 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 903 903 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 964 964 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 1017 1017 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
MOD_RES 1044 1044 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1076 1076 Phosphoserine.
{ECO:0000250|UniProtKB:Q14C86}.
VAR_SEQ 373 379 GCVAAFL -> VGMSVVS (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_032363.
VAR_SEQ 380 1458 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_032364.
VAR_SEQ 480 480 I -> IGQQLAAITAWDSSATNLTAHIPLVTPF (in
isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_032365.
VAR_SEQ 557 577 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14621295,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:17189207}.
/FTId=VSP_032366.
VAR_SEQ 1055 1055 Missing (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_032367.
VAR_SEQ 1202 1202 Missing (in isoform 5).
{ECO:0000303|PubMed:14621295}.
/FTId=VSP_032368.
CONFLICT 581 581 N -> D (in Ref. 3; BAE29251).
{ECO:0000305}.
CONFLICT 661 661 G -> E (in Ref. 5; AAH31478).
{ECO:0000305}.
CONFLICT 893 893 Y -> H (in Ref. 3; BAE22277).
{ECO:0000305}.
CONFLICT 1257 1257 A -> V (in Ref. 2; BAC98191).
{ECO:0000305}.
SEQUENCE 1458 AA; 162402 MW; CA3D2EAF22051FD7 CRC64;
MVKLDIHTLA HHLKQERLYV SSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII
TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL
NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI
LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPAQ QEKLFGEKGS
DRFRQKVQEM VDSNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG
EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGTEEGD
PRTKNSLGKF DKGCVAAFLD VVIGGRAVET PPMSSVNLLE GLSRTVVYIS YSQLITLVNF
MKSVMSGDQL KEDRMALDNL LANLPQAKPG KSSSLDMTPY STPQMSPATT PANKKNRLPI
ATRSRSRSNM LMDLHMDHEG SSQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL
SDGGQGDVPV DENKLHGKPD KTLRFSLCSD NLEGISEGPS NRSNSVSSLD LEGESVSELG
AGPSGSNGVE ALQLLEHEQA TTQDNLDDKL RKFEIRDMMG LTDDRDISET VSETWSTDVL
GSDFDPNVDE DRLQEIAGAA AENVLGSLLC LPGSGSVLLD PCTGSTISET TSEAWSVEVL
PSDSEAPDLK QEERLQELES CSGLGSTSDD TDVREVSSRP STPGLSVVSG ISATSEDIPN
KIEDLRSECS SDFGGKDSVT SPDMDDIAHG AHQLTSPPSQ SESLLAMFDP LSSHEGASAV
VRPKVHYARP SHPPPDPPIL EGAVGGNEAR LPNFGSHVLT AAEMEAFKQR HSYPERLVRS
RSSDIVSSVR RPMSDPSWNR RPGNEELPPA AATGATSLVA APHSSSSSPS KDSSRGETEE
RKDSDDERSD RSRPWWRKRF VSAMPKAPIP FRKKEKQEKD KDDLGPDRFS TLTDEPSPRL
SAQAQVAEDI LDKYRNAIKR TSPSEGAMAN DESAEVMGDG ESAHDSPREE ALQNISADDL
PDSASQAAHP QDSAFSYRDV KKKLRLALCS ADSVAFPVLT HSTRNGLPDH TDPEDNEIVC
FLKVQIAEAI NLQDKSLMAQ LQETMRCVCR FDNRTCRKLL ASIAEDYRKR APYIAYLTRC
RQGLQTTQAH LERLLQRVLR DKEVANRYFT TVCVRLLLES KEKKIREFIQ DFQKLTAADD
KTAQVEDFLQ FLYGVMAQDV IWQNASEEQL QDAQLAIERS VMNRIFKLAF YPNQDGDILR
DQVLHEHIQR LSKVVTANHR ALQIPEVYLR EAPWPSAQSE IRTISAYKTP RDKVQCILRM
CSTIMNLLSL ANEDSVPGAD DFVPVLVFVL IKANPPCLLS TVQYISSFYA SCLSGEESYW
WMQFTAAVEF IKTIDDRK


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