TRIO_RAT
ID TRIO_RAT Reviewed; 3100 AA.
AC F1M0Z1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 4.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Triple functional domain protein;
DE EC=2.7.11.1;
DE AltName: Full=PTPRF-interacting protein;
GN Name=Trio;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627; SER-1632; SER-1633;
RP THR-1824; SER-2283; SER-2459 AND SER-2463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=26721934; DOI=10.1093/hmg/ddv618;
RA Ba W., Yan Y., Reijnders M.R., Schuurs-Hoeijmakers J.H., Feenstra I.,
RA Bongers E.M., Bosch D.G., De Leeuw N., Pfundt R., Gilissen C.,
RA De Vries P.F., Veltman J.A., Hoischen A., Mefford H.C., Eichler E.E.,
RA Vissers L.E., Nadif Kasri N., De Vries B.B.;
RT "TRIO loss of function is associated with mild intellectual disability and
RT affects dendritic branching and synapse function.";
RL Hum. Mol. Genet. 25:892-902(2016).
RN [4]
RP INTERACTION WITH BSN AND PCLO.
RX PubMed=27907191; DOI=10.1371/journal.pone.0167535;
RA Terry-Lorenzo R.T., Torres V.I., Wagh D., Galaz J., Swanson S.K.,
RA Florens L., Washburn M.P., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Trio, a Rho Family GEF, Interacts with the Presynaptic Active Zone
RT Proteins Piccolo and Bassoon.";
RL PLoS ONE 11:E0167535-E0167535(2016).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1
CC GTPases. Involved in coordinating actin remodeling, which is necessary
CC for cell migration and growth (By similarity). Plays a key role in the
CC regulation of neurite outgrowth and lamellipodia formation (By
CC similarity). In developing hippocampal neurons, limits dendrite
CC formation, without affecting the establishment of axon polarity. Once
CC dendrites are formed, involved in the control of synaptic function by
CC regulating the endocytosis of AMPA-selective glutamate receptors
CC (AMPARs) at CA1 excitatory synapses (PubMed:26721934). May act as a
CC regulator of adipogenesis (By similarity).
CC {ECO:0000250|UniProtKB:O75962, ECO:0000250|UniProtKB:Q0KL02,
CC ECO:0000269|PubMed:26721934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with CARMIL1 (By similarity). Interacts with
CC PTPRF/LAR (By similarity). Interacts with ANKRD26 (By similarity).
CC Interacts with Bassoon/BSN and Piccolo/PCLO (PubMed:27907191).
CC Interacts with the cytoplasmic region of the heterodimer formed by NGFR
CC and SORCS2. ProNGF binding mediates dissociation of TRIO from the
CC receptor complex (By similarity). {ECO:0000250|UniProtKB:O75962,
CC ECO:0000269|PubMed:27907191}.
CC -!- INTERACTION:
CC F1M0Z1; Q62765: Nlgn1; NbExp=2; IntAct=EBI-26961238, EBI-7281118;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0KL02}. Cell
CC projection {ECO:0000250|UniProtKB:Q0KL02}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during the early postnatal period
CC (P1 to P7) in the hippocampus. At P11, levels start to decrease rapidly
CC until p19 and then more progressively until adulthood (at protein
CC level). {ECO:0000269|PubMed:26721934}.
CC -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes nucleotide
CC exchange for RAC1, leading to the activation of Jun kinase and the
CC production of membrane ruffles. The second DBL/GEF domain is an
CC exchange factor for rhoa and induces the formation of stress fibers.
CC {ECO:0000250|UniProtKB:O75962}.
CC -!- PTM: Phosphorylated on serine residue(s).
CC {ECO:0000250|UniProtKB:O75962}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AABR07008947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07008948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006232152.1; XM_006232090.3.
DR SMR; F1M0Z1; -.
DR IntAct; F1M0Z1; 15.
DR MINT; F1M0Z1; -.
DR STRING; 10116.ENSRNOP00000016784; -.
DR iPTMnet; F1M0Z1; -.
DR PhosphoSitePlus; F1M0Z1; -.
DR PaxDb; F1M0Z1; -.
DR PRIDE; F1M0Z1; -.
DR GeneID; 310192; -.
DR UCSC; RGD:1308360; rat.
DR CTD; 7204; -.
DR RGD; 1308360; Trio.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG4240; Eukaryota.
DR HOGENOM; CLU_000373_1_0_1; -.
DR InParanoid; F1M0Z1; -.
DR OrthoDB; 5761at2759; -.
DR TreeFam; TF318080; -.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:F1M0Z1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.900.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR028570; Kalirin/TRIO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF104; PTHR22826:SF104; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF48065; SSF48065; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Disulfide bond;
KW Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..3100
FT /note="Triple functional domain protein"
FT /id="PRO_0000438732"
FT DOMAIN 65..210
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 311..418
FT /note="Spectrin 1"
FT REPEAT 538..644
FT /note="Spectrin 2"
FT REPEAT 878..984
FT /note="Spectrin 3"
FT REPEAT 1109..1216
FT /note="Spectrin 4"
FT DOMAIN 1292..1467
FT /note="DH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1479..1591
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1656..1721
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1970..2146
FT /note="DH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2158..2272
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 2556..2621
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 2686..2776
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2797..3051
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2288..2557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2644..2668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2355..2390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2401..2418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2425..2440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2485..2513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2528..2557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2916
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2803..2811
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2826
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1824
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75962"
FT DISULFID 2707..2760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 3100 AA; 347860 MW; CF2D837E3D091509 CRC64;
MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM
KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRMR QEDLRRLISY LACIPSEEVC
KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHIALIIK PDNFWQKQRT NFGSSKFEFE
TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EDYISNAAHM LSRLEELQDV
LAKKELPQDL EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE SFPKKNSGSG
NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK
GLFLNSYTEI GASHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIK
QIANQLEQEW KAFAAALDER STLLDMSSIF HQKAEKYMSN VDSWCKACGE VDLPSELQDL
EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV
IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV
RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT
LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSINHIETV LQQLDEAQSQ MEELFQERKI
KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN
LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT
HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS
EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN
ADVFLKYLHR NSVSMPGMVT HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY
VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ
LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF
QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL
TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA LKEPIHIPKT APAARQKGRR
DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSNELTIRRG
QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS
SNDASPPASV ASLQPHMMGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH
KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS GMQSCGEEEG
EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS SETPSAAELV SAIEELVKSK
MALEDRPSSL LVDQGDSSSP SFNPSDNSLL SSSSPIDEME ERKCSLSLKR RHYVLQELVE
TERDYVRDLG CVVEGYMALM KEDGVPDDMK GKDKIVFGNI HQIYDWHRDF FLGELEKCLE
DPEKLGSLFV KHERRLHMYI VYCQNKPKSE HIVSEYIDTF FEDLKQRLGH RLQLTDLLIK
PVQRIMKYQL LLKDFLKYSK KASLDTSELE KAVEVMCIVP KRCNDMMNVG RLQGFDGKIV
AQGKLLLQDT FLVTDQDAGL LPRCKERRVF LFEQIVIFSE PLDKKKGFSM PGFLFKNSIK
VSCLCLEENV ESDPCKFALT SRTGDAVETF ILHSSSPSVR QTWIHEINQI LENQRNFLNA
LTSPIEYQRN HSGGGGSGSG GSSGGGGGSG GSGASSGGSS SHGSGPSSCS SGPSSSRSRP
SRIPQPVRHH PPMLVSSAAS SQAEADKMSG MSAPSPSLPT PSNSLALEAS LGQPSRLPLS
GDSEGHERET EPIPKMKVME SPRKALGSTS GTSQDGNTKD ARGNLGPLPL GKTRPGAVSP
LNSPLSTTFP SPFGKEAFPP SSPLQKGGSF WSSIPASPAS RPSSFTFPGD SDSLQRQTHR
HAAPSKDTDR MSTCSSASEQ SVQSTQSNGS ESSSSSNIST MLVTHEYTAV KEDEINVYQG
EVVQILASNQ QNMFLVFRAA TDQCPAAEGW IPGFVLGHTS AVIMENPDGT FKKSTSWHTA
LRLRKKSEKK DKDGKRDGKL ENGYRKPREG LSNKLLNPNY IYDVPPEFVI PLSEVTCETG
ETVVFRCRVC GRPKASITWK GPEHNTLNND DHYNISYSDV GEATLKIIGV STEDDGVYTC
IAVNDMGSAS SSASLRVLGP GSDGIVVTWK DNFDAFYSEV AELGRGRFAV VKKCDQKGTK
RAVATKFVNK KLMKRDQVTH ELGILQNLQH PLFVSLLDTF ETPTSYVLVL ELADQGRLLD
CVVRWGSLTE GKVRAHLGEV LEAVRYLHNC RIAHLDLKPE NILVDQSLAK PTIKLTDFGD
AVQLNTTYYI HQLLGNPEFA APEIILGNPV SLTADTWSVG VLTYVLLSGV SPFLDDSVEE
TCLNICRLDF SFPEDYFQGV SQKAKEFVCF LLQEDPAKRP SAALALQEQW LQAGNGSGKG
MGVLDTSRLT SFIERRKHQN DVRPIRSIKN FLQSRLLPRV
