ARAP1_MOUSE
ID ARAP1_MOUSE Reviewed; 1452 AA.
AC Q4LDD4; B2RUJ3; Q3UDD2; Q3US99; Q58ET6; Q6PEQ9; Q6ZQ48;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=Centaurin-delta-2 {ECO:0000250|UniProtKB:Q96P48};
DE Short=Cnt-d2 {ECO:0000250|UniProtKB:Q96P48};
GN Name=Arap1 {ECO:0000312|MGI:MGI:1916960};
GN Synonyms=Centd2 {ECO:0000312|EMBL:AAI41180.1, ECO:0000312|MGI:MGI:1916960},
GN Kiaa0782 {ECO:0000312|EMBL:BAC98023.1};
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:CAF21318.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Krugmann S., Coadwell J., Stephens L.R., Hawkins P.T.;
RT "ARAP1 splice variants in man and mouse.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE23358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23358.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAE23358.1},
RC Bone marrow macrophage {ECO:0000312|EMBL:BAE29329.1}, and
RC Cerebellum {ECO:0000312|EMBL:BAE24434.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAI41180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1320-1452 (ISOFORM 2/3).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH57922.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAI41180.1}, and
RC Liver {ECO:0000312|EMBL:AAH57922.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAC98023.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1452 (ISOFORM 2/3).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC98023.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, 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: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-
CC activating protein that modulates actin cytoskeleton remodeling by
CC regulating ARF and RHO family members. Is activated by
CC phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can
CC be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2)
CC binding, albeit with lower efficiency. Has a preference for ARF1 and
CC ARF5 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TNFRSF10A. {ECO:0000250|UniProtKB:Q96P48}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96P48}. Golgi
CC apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q96P48};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q96P48}. Cell
CC membrane {ECO:0000250|UniProtKB:Q96P48}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q4LDD4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q4LDD4-2; Sequence=VSP_053048;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q4LDD4-3; Sequence=VSP_053047, VSP_053048;
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DR EMBL; AJ621558; CAF21318.1; -; mRNA.
DR EMBL; AK137455; BAE23358.1; -; mRNA.
DR EMBL; AK140646; BAE24434.1; -; mRNA.
DR EMBL; AK150132; BAE29329.1; -; mRNA.
DR EMBL; BC057922; AAH57922.1; -; mRNA.
DR EMBL; BC091762; AAH91762.1; -; mRNA.
DR EMBL; BC141179; AAI41180.1; -; mRNA.
DR EMBL; AK129213; BAC98023.1; -; mRNA.
DR CCDS; CCDS21510.1; -. [Q4LDD4-3]
DR CCDS; CCDS40041.1; -. [Q4LDD4-2]
DR RefSeq; NP_001035200.1; NM_001040111.1. [Q4LDD4-2]
DR RefSeq; NP_001035201.1; NM_001040112.1. [Q4LDD4-3]
DR RefSeq; NP_081456.2; NM_027180.3. [Q4LDD4-3]
DR RefSeq; NP_932764.1; NM_198096.1.
DR RefSeq; XP_006508249.1; XM_006508186.3. [Q4LDD4-1]
DR RefSeq; XP_006508250.1; XM_006508187.1. [Q4LDD4-1]
DR RefSeq; XP_006508251.1; XM_006508188.3. [Q4LDD4-1]
DR RefSeq; XP_011240199.1; XM_011241897.2. [Q4LDD4-1]
DR PDB; 5XHZ; X-ray; 1.32 A; C/D=80-90.
DR PDBsum; 5XHZ; -.
DR AlphaFoldDB; Q4LDD4; -.
DR SMR; Q4LDD4; -.
DR BioGRID; 213630; 1.
DR IntAct; Q4LDD4; 1.
DR STRING; 10090.ENSMUSP00000102624; -.
DR iPTMnet; Q4LDD4; -.
DR PhosphoSitePlus; Q4LDD4; -.
DR SwissPalm; Q4LDD4; -.
DR EPD; Q4LDD4; -.
DR jPOST; Q4LDD4; -.
DR MaxQB; Q4LDD4; -.
DR PaxDb; Q4LDD4; -.
DR PeptideAtlas; Q4LDD4; -.
DR PRIDE; Q4LDD4; -.
DR ProteomicsDB; 296277; -. [Q4LDD4-1]
DR ProteomicsDB; 296278; -. [Q4LDD4-2]
DR ProteomicsDB; 296279; -. [Q4LDD4-3]
DR Antibodypedia; 30876; 185 antibodies from 30 providers.
DR Ensembl; ENSMUST00000084895; ENSMUSP00000081957; ENSMUSG00000032812. [Q4LDD4-3]
DR Ensembl; ENSMUST00000084896; ENSMUSP00000081958; ENSMUSG00000032812. [Q4LDD4-1]
DR Ensembl; ENSMUST00000107010; ENSMUSP00000102624; ENSMUSG00000032812. [Q4LDD4-2]
DR GeneID; 69710; -.
DR KEGG; mmu:69710; -.
DR UCSC; uc009iok.1; mouse. [Q4LDD4-2]
DR UCSC; uc009iol.1; mouse. [Q4LDD4-1]
DR UCSC; uc009iom.1; mouse. [Q4LDD4-3]
DR CTD; 116985; -.
DR MGI; MGI:1916960; Arap1.
DR VEuPathDB; HostDB:ENSMUSG00000032812; -.
DR eggNOG; KOG1117; Eukaryota.
DR GeneTree; ENSGT00940000157424; -.
DR HOGENOM; CLU_002900_1_1_1; -.
DR InParanoid; Q4LDD4; -.
DR OMA; SVIKAGW; -.
DR OrthoDB; 98944at2759; -.
DR PhylomeDB; Q4LDD4; -.
DR TreeFam; TF105769; -.
DR Reactome; R-MMU-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 69710; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Arap1; mouse.
DR PRO; PR:Q4LDD4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q4LDD4; protein.
DR Bgee; ENSMUSG00000032812; Expressed in granulocyte and 166 other tissues.
DR ExpressionAtlas; Q4LDD4; baseline and differential.
DR Genevisible; Q4LDD4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 3.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 5.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Golgi apparatus; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1452
FT /note="Arf-GAP with Rho-GAP domain, ANK repeat and PH
FT domain-containing protein 1"
FT /id="PRO_0000367029"
FT DOMAIN 6..70
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 329..421
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 442..531
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 537..662
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 745..852
FT /note="PH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 956..1141
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 1174..1263
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 1276..1398
FT /note="PH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 552..575
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 87..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P48"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P48"
FT MOD_RES 506
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P48"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P48"
FT MOD_RES 1430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P48"
FT MOD_RES 1437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..248
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053047"
FT VAR_SEQ 1322..1332
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053048"
FT CONFLICT 153
FT /note="P -> S (in Ref. 3; AAI41180)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> A (in Ref. 3; AAI41180)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="V -> G (in Ref. 1; CAF21318)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="T -> R (in Ref. 3; AAH57922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1452 AA; 162276 MW; 1606F3534555D4F6 CRC64;
MAEGYDAALS VAEWLRALHL EQYTALFEQH GLVWATECQG LSDAGLLDMG MHLPGHRRRI
LAGLHRAHAP PVPLPRPAPR PVPMKRHIFR SPPVPVTPPE PPPTAGEDEG LPAAPPIPPR
RSCLPPACFT PTSTAAPDPV LPPLPAKRHL VEPSVPPVPP RTGPPYPQAS LLAKEELLLP
SVSPRSQPEP AETPSTLLPA FPQGPLQPPS PPPCPPVIPP KPPRLLPEFD DSDYDDVPEE
GPGAPASVMT KEEPLPSRVP RAVRVASLLS EGEELSGDDS EDDDDHAYEG IPNGGWPTSG
LNPPLRSLIP DLPLHPMDEL PGGPTPITPV IKAGWLDKNP PQGSYIYQKR WVRLDADYLR
YFDSNKDAYS KRFVPVACIC RVAPIGDQKF EVITNNRTFA FRAESDVERN EWMQALQQAV
VEHRARFRLS SASVLGVRGS EQPDRAGSLE LRGFKNKLYV AVTGDKVQLY KNLEEFHLGI
GITFIDMNVG NVKEVDRRSF DLTTPYRIFS FSADSELEKE QWLEAMQGAI AEALSTSEVA
ERIWAAAPNR FCADCGAAQP DWASINLCVV ICKRCAGEHR GLGAGVSKVR SLKMDRKVWT
EALIQLFLHL GNGPGNHFWA ANVPPSEALE PSSSPGARRY HLEAKYREGK YRRYHPLFGN
QEELDKALCA AVTTTDLAET QALLGCGAGV SCFSGDPAAP TPLALAEQAG QTLQMEFLRN
NQSTEVPRLD SVKPLEKHYS VTLPTVSHSG FLYKTASAGK PLQDRRAREE FSRRWCVLSD
GVLSYYENER AVTPNGEIRA SEIVCLAVSP LDTHGFEHTF EVYTEGERLY LFGLENAELA
HEWVKCIAKA FVPPLAEDLL ARDFERLGRL PCKAGLSLQQ AQEGWFALTG SELRAVFPEG
PWEEPLQLRK LQELSIQGDS ENQVLVLVER RRTLYIQGER RLDFMAWLGV IQKAAASLGD
TLSEQQLGDS DIPVIVYRCV DYITQCGLTS EGIYRKCGQT SKTQRLLDSL RQDARSVHLK
EGEQHVDDVS SALKRFLRDL PDGLFTRAQR LAWLEASEIE DEEEKISRYR ELLVHLPPVN
RATVKALISH LYCVQCFSDT NQMNTHNLAI VFGPTLFQTD GQDYKAGKVV EDLINHYVVV
FSVDEEELRK QREEVTAIVK MRVAGTASGT QHAGDFICTV YLEEKKVETE QHVKIPASMT
AEELTLEILD RRNVSIREKD YWTCFEVNEK EEAERPLHFA EKVLPIVHGL GIDSHLVVKK
YQSMEAMLLY LASRVGDTKH GMMKFREDRS LLGLGLPSGG FHDRYFILNS SCLRLYKEVR
SQRPWSGAPE TSHRPEKEWP VKSLKVYLGV KKKLRPPTCW GFTVVHETEK HEKQQWYLCC
DTQMELREWF ATFLSVQHDG LVWPSEPSRV SRAVPEVRMG SVSLIPLRGS ENEMRRSVAA
FTADPLSLLR HV
