RBG1L_MOUSE
ID RBG1L_MOUSE Reviewed; 815 AA.
AC A6H6A9; Q3UH20; Q80TZ4; Q8BZD2; Q8BZP0; Q8CFI6; Q9QY69;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Rab GTPase-activating protein 1-like;
GN Name=Rabgap1l {ECO:0000312|MGI:MGI:1352507};
GN Synonyms=Hhl {ECO:0000312|EMBL:AAF24092.1},
GN Kiaa0471 {ECO:0000312|EMBL:BAC65574.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC29189.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29189.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAE28037.1},
RC Cerebellum {ECO:0000312|EMBL:BAC29189.1}, and
RC Diencephalon {ECO:0000312|EMBL:BAC28549.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAI45812.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH38651.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAI45812.1}, and
RC Thymus {ECO:0000312|EMBL:AAH38651.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF24092.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-386 (ISOFORMS 1/3), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1 X 129/Sv {ECO:0000312|EMBL:AAF24092.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:AAF24092.1};
RX PubMed=10585558; DOI=10.1016/s0925-4773(99)00234-8;
RA Hidaka M., Caruana G., Stanford W.L., Sam M., Correll P.H., Bernstein A.;
RT "Gene trapping of two novel genes, Hzf and Hhl, expressed in hematopoietic
RT cells.";
RL Mech. Dev. 90:3-15(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC65574.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 790-815 (ISOFORM 3).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65574.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [7]
RP FUNCTION, INTERACTION WITH ANK2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF ARG-584 AND 784-LYS-LYS-785.
RX PubMed=27718357; DOI=10.7554/elife.20417;
RA Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT recycling via recruiting RabGAP1L to early endosomes.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase
CC RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP
CC (By similarity). Plays a role in endocytosis and intracellular protein
CC transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate
CC (PI3P)-positive early endosomes, where it inactivates RAB22A, and
CC promotes polarized trafficking to the leading edge of the migrating
CC cells. Part of the ANK2/RABGAP1L complex which is required for the
CC polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma
CC membrane that enables continuous directional cell migration
CC (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372,
CC ECO:0000269|PubMed:27718357}.
CC -!- SUBUNIT: Interacts (via Rab-GAP TBC domain) with ANK2 (via death
CC domain). {ECO:0000269|PubMed:27718357}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:27718357}.
CC Golgi apparatus {ECO:0000250|UniProtKB:Q5R372}. Note=Colocalizes on
CC endosomes partially with EEA1 (By similarity). Colocalizes and
CC cotransports on motile vesicles with ANK2 (PubMed:27718357).
CC {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=A6H6A9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=A6H6A9-2; Sequence=VSP_052927, VSP_052928, VSP_052929;
CC Name=3 {ECO:0000269|PubMed:12693553, ECO:0000269|PubMed:16141072};
CC IsoId=A6H6A9-3; Sequence=VSP_052926, VSP_052930, VSP_052932;
CC Name=4 {ECO:0000269|PubMed:15489334};
CC IsoId=A6H6A9-4; Sequence=VSP_052925, VSP_052931;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic heart and liver, and in
CC hemopoietic cells (PubMed:10585558). Expressed in the corpus callosum
CC in the central nervous system (CNS) and costameres in skeletal muscle
CC at postnatal day (PND) 30 (PubMed:27718357).
CC {ECO:0000269|PubMed:10585558, ECO:0000269|PubMed:27718357}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24092.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF24092.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF24092.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK034019; BAC28549.1; -; mRNA.
DR EMBL; AK035796; BAC29189.1; -; mRNA.
DR EMBL; AK147634; BAE28037.1; -; mRNA.
DR EMBL; BC038651; AAH38651.1; -; mRNA.
DR EMBL; BC145811; AAI45812.1; -; mRNA.
DR EMBL; BC145813; AAI45814.1; -; mRNA.
DR EMBL; AF118565; AAF24092.1; ALT_SEQ; mRNA.
DR EMBL; AK122292; BAC65574.1; -; mRNA.
DR CCDS; CCDS15407.1; -. [A6H6A9-3]
DR CCDS; CCDS15408.1; -. [A6H6A9-1]
DR RefSeq; NP_001033710.1; NM_001038621.2. [A6H6A9-3]
DR RefSeq; NP_038890.3; NM_013862.5. [A6H6A9-1]
DR RefSeq; XP_006496946.1; XM_006496883.3. [A6H6A9-4]
DR AlphaFoldDB; A6H6A9; -.
DR SMR; A6H6A9; -.
DR BioGRID; 205890; 1.
DR STRING; 10090.ENSMUSP00000028049; -.
DR iPTMnet; A6H6A9; -.
DR PhosphoSitePlus; A6H6A9; -.
DR EPD; A6H6A9; -.
DR MaxQB; A6H6A9; -.
DR PaxDb; A6H6A9; -.
DR PeptideAtlas; A6H6A9; -.
DR PRIDE; A6H6A9; -.
DR ProteomicsDB; 255032; -. [A6H6A9-1]
DR ProteomicsDB; 255033; -. [A6H6A9-2]
DR ProteomicsDB; 255034; -. [A6H6A9-3]
DR ProteomicsDB; 255035; -. [A6H6A9-4]
DR Antibodypedia; 34402; 80 antibodies from 21 providers.
DR DNASU; 29809; -.
DR Ensembl; ENSMUST00000028049; ENSMUSP00000028049; ENSMUSG00000026721. [A6H6A9-1]
DR Ensembl; ENSMUST00000028052; ENSMUSP00000028052; ENSMUSG00000026721. [A6H6A9-3]
DR Ensembl; ENSMUST00000195442; ENSMUSP00000141666; ENSMUSG00000026721. [A6H6A9-2]
DR GeneID; 29809; -.
DR KEGG; mmu:29809; -.
DR UCSC; uc007deh.1; mouse. [A6H6A9-3]
DR UCSC; uc007dej.2; mouse. [A6H6A9-1]
DR UCSC; uc007dek.1; mouse. [A6H6A9-2]
DR CTD; 9910; -.
DR MGI; MGI:1352507; Rabgap1l.
DR VEuPathDB; HostDB:ENSMUSG00000026721; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000154611; -.
DR HOGENOM; CLU_022409_1_0_1; -.
DR InParanoid; A6H6A9; -.
DR OMA; XDSAQES; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; A6H6A9; -.
DR TreeFam; TF317184; -.
DR BioGRID-ORCS; 29809; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Rabgap1l; mouse.
DR PRO; PR:A6H6A9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A6H6A9; protein.
DR Bgee; ENSMUSG00000026721; Expressed in lumbar dorsal root ganglion and 244 other tissues.
DR ExpressionAtlas; A6H6A9; baseline and differential.
DR Genevisible; A6H6A9; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0035855; P:megakaryocyte development; NAS:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
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 InterPro; IPR042809; RABGAP1L.
DR PANTHER; PTHR22957:SF205; PTHR22957:SF205; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
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 Alternative splicing; Endocytosis; Endosome; Golgi apparatus;
KW GTPase activation; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..815
FT /note="Rab GTPase-activating protein 1-like"
FT /id="PRO_0000348055"
FT DOMAIN 126..282
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 538..724
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 84..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 580
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 621
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5R372"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5R372"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..743
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052925"
FT VAR_SEQ 1..681
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052926"
FT VAR_SEQ 1..30
FT /note="MEVRASFQKVSGSSDSVATLNSEEFVLVSQ -> ME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052927"
FT VAR_SEQ 489..505
FT /note="ESDNELSSGTGDVSKDC -> DPGHASPDTVGFLTLFL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052928"
FT VAR_SEQ 506..815
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052929"
FT VAR_SEQ 682..737
FT /note="YSHFCDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVAL
FT ALLK -> MEEGVPCPAPAAKLTPPVKKSQDMHDERSKLVNEYACRVLELLGMGHRLFV
FT PRLLA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052930"
FT VAR_SEQ 744..780
FT /note="LQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIK -> MMEEISIMVAY
FT DAHVFSQLHDEDFLTSLVATSKPRSM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052931"
FT VAR_SEQ 812..815
FT /note="FVYL -> RENRRLQEASMRLEQENDDLAHELVTSKIALRNDLDQAEDKADV
FT LNKELLFTKQRLVETEEEKRKQEEETAQLKEVFRKQLEKAEYEIKKTTAIIAEYKQICS
FT QLSTRLEKQQAASKEELEAVKGKMMACKHCSDIFSKEGALKPVAVNREDQGLEADDEKD
FT SLKKQLREMELELAQTKLQLVEAKCKIQELEHQRGALMNEIQAAKNSWFSKTLNSIKTA
FT TGTQPLQPPQAPQPPKEST (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052932"
FT MUTAGEN 584
FT /note="R->A: Loss GTPase-activating (GAP) activity."
FT /evidence="ECO:0000269|PubMed:27718357"
FT MUTAGEN 784..785
FT /note="KK->EE: Loss of interaction with ANK2. Loss of
FT colocalization and cotransportation on motile vesicles with
FT ANK2."
FT /evidence="ECO:0000269|PubMed:27718357"
FT CONFLICT 4
FT /note="R -> G (in Ref. 3; AAF24092)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="S -> C (in Ref. 1; BAC29189)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="G -> E (in Ref. 3; AAF24092)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> I (in Ref. 3; AAF24092)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..386
FT /note="PKD -> LSQ (in Ref. 3; AAF24092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 92404 MW; 28AA916BF9BA3F0E CRC64;
MEVRASFQKV SGSSDSVATL NSEEFVLVSQ HTDATSIKDD GKPQLKIASN GDEQLEKAME
EILRDSEKGQ SGLPVDCQGS SEISDCPFGD VPASQTTKPP LQLILDPSNT EISTPRPSSP
SRFPEEDSVL FNKLTYLGCM KVSSPRSEVE ALRAMATMRA SSQYPFAVTL YVPNVPEGSV
RIIDQSSNVE IASFPIYKVL FCARGHDGTA ESNCFAFTES SHGSEEFQIH VFSCEIKEAV
SRILYSFCTA FKRSSRQVSD VKDSVIPTPD SDVFTFSVSL EVKEDDGKGN FSPVPKDRDK
FYFKIKQGIE KKVVITVQQL SNKELAIERC FGMLLSPGRN VKNSDMHLLD MESMGKSYDG
RAYVITGMWN PNAPIFLALN EETPKDKRVY MTVAVDMVVT EVVEPVRFLL ETVVRVYPAN
ERFWYFSRKT FTETFFMRLK QSEGKGHSSA GDAIYEVVSL QRESDKEEPI TPTSAGGPMS
PQEDEAEEES DNELSSGTGD VSKDCPEKIL YSWGELLGRW HNNLGGRPKG LFTLVKSGVP
EALRAEVWQL LAGCHDNQEM LDKYRILITK DSAQESVITR DIHRTFPAHD YFKDTGGDGQ
ESLYKICKAY SVFDEDIGYC QGQSFLAAVL LLHMPEEQAF CVLVTIMYGY KLRDLYRNNF
EDLHCKFYQL EKLMQEQLPD LYSHFCDLNL EAHMYASQWF LTLFTAKFPL CMVFHIIDLL
LCEGLNIIFH VALALLKTSK EDLLQADFEG ALKFFRVQLP KRYRAEENAR RLMEQACNIK
VPTKKLKKYE KEYQAMRENQ LQQEDPMDRY KFVYL
