ID KIF1B_MOUSE Reviewed; 1816 AA.
AC Q60575; Q9R0B4; Q9WVE5; Q9Z119;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=Kinesin-like protein KIF1B;
GN Name=Kif1b;
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 [MRNA] (ISOFORM 3), AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=7528108; DOI=10.1016/0092-8674(94)90012-4;
RA Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R., Yamazaki H.,
RA Hirokawa N.;
RT "KIF1B, a novel microtubule plus end-directed monomeric motor protein for
RT transport of mitochondria.";
RL Cell 79:1209-1220(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10571041; DOI=10.1016/s0378-1119(99)00370-4;
RA Gong T.L., Winnicki R.S., Kohrman D.C., Lomax M.I.;
RT "A novel kinesin of the UNC-104/KIF1 subfamily encoded by the Kif1b gene.";
RL Gene 239:117-127(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10341097; DOI=10.1007/s003359901056;
RA Conforti L., Buckmaster E.A., Tarlton A., Brown M.C., Lyon M.F.,
RA Perry V.H., Coleman M.P.;
RT "The major brain isoform of kif1b lacks the putative mitochondria-binding
RT domain.";
RL Mamm. Genome 10:617-622(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ICR;
RA Nakagawa T., Hirokawa N.;
RT "Identification and characterization of a new kinesin superfamily KIF1B-
RT beta.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1487, AND IDENTIFICATION BY
RP 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-1454, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP INTERACTION WITH MADD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18849981; DOI=10.1038/ncb1785;
RA Niwa S., Tanaka Y., Hirokawa N.;
RT "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL Nat. Cell Biol. 10:1269-1279(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-647; THR-652; SER-1454 AND
RP SER-1487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
CC -!- FUNCTION: Motor for anterograde transport of mitochondria. Has a
CC microtubule plus end-directed motility.
CC -!- FUNCTION: Isoform 1 mediates the transport of synaptic vesicles in
CC neuronal cells. {ECO:0000250|UniProtKB:O88658}.
CC -!- SUBUNIT: Monomer (PubMed:7528108). Interacts with KIFBP (By
CC similarity). Interacts (via C-terminus end of the kinesin-motor domain)
CC with CHP1; the interaction occurs in a calcium-dependent manner (By
CC similarity). Interacts with MADD (via death domain) (PubMed:18849981).
CC {ECO:0000250|UniProtKB:O60333, ECO:0000250|UniProtKB:O88658,
CC ECO:0000269|PubMed:18849981, ECO:0000269|PubMed:7528108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Mitochondrion
CC {ECO:0000250|UniProtKB:O60333}. Cell projection, axon
CC {ECO:0000269|PubMed:18849981}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle {ECO:0000250|UniProtKB:O88658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q60575-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q60575-2; Sequence=VSP_002862, VSP_002863;
CC Name=3;
CC IsoId=Q60575-3; Sequence=VSP_002862, VSP_002863, VSP_002864,
CC VSP_002865;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:18849981}.
CC -!- DISRUPTION PHENOTYPE: Reduced Rab3 and Madd levels in distal axons of
CC hippocampal neurons. {ECO:0000269|PubMed:18849981}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; D17577; BAA04503.1; -; mRNA.
DR EMBL; AF090190; AAF06718.1; -; mRNA.
DR EMBL; AF131865; AAD39438.1; -; mRNA.
DR EMBL; AB023656; BAA75243.1; -; mRNA.
DR CCDS; CCDS18956.1; -. [Q60575-2]
DR CCDS; CCDS18957.1; -. [Q60575-3]
DR CCDS; CCDS71521.1; -. [Q60575-1]
DR PIR; A55289; A55289.
DR RefSeq; NP_001277924.1; NM_001290995.1. [Q60575-1]
DR RefSeq; NP_032467.2; NM_008441.2.
DR AlphaFoldDB; Q60575; -.
DR SMR; Q60575; -.
DR BioGRID; 200936; 11.
DR IntAct; Q60575; 6.
DR STRING; 10090.ENSMUSP00000056754; -.
DR GlyGen; Q60575; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q60575; -.
DR PhosphoSitePlus; Q60575; -.
DR SwissPalm; Q60575; -.
DR EPD; Q60575; -.
DR jPOST; Q60575; -.
DR MaxQB; Q60575; -.
DR PaxDb; 10090-ENSMUSP00000061472; -.
DR PeptideAtlas; Q60575; -.
DR ProteomicsDB; 263600; -. [Q60575-1]
DR ProteomicsDB; 263601; -. [Q60575-2]
DR ProteomicsDB; 263602; -. [Q60575-3]
DR Pumba; Q60575; -.
DR Antibodypedia; 4196; 140 antibodies from 24 providers.
DR DNASU; 16561; -.
DR Ensembl; ENSMUST00000055647.15; ENSMUSP00000061472.9; ENSMUSG00000063077.16. [Q60575-2]
DR Ensembl; ENSMUST00000060537.13; ENSMUSP00000056754.7; ENSMUSG00000063077.16. [Q60575-1]
DR GeneID; 16561; -.
DR KEGG; mmu:16561; -.
DR UCSC; uc008vvy.2; mouse. [Q60575-2]
DR UCSC; uc008vvz.2; mouse. [Q60575-1]
DR AGR; MGI:108426; -.
DR CTD; 23095; -.
DR MGI; MGI:108426; Kif1b.
DR VEuPathDB; HostDB:ENSMUSG00000063077; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000157445; -.
DR HOGENOM; CLU_001485_10_0_1; -.
DR InParanoid; Q60575; -.
DR OMA; IKITICH; -.
DR OrthoDB; 126886at2759; -.
DR PhylomeDB; Q60575; -.
DR TreeFam; TF105221; -.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16561; 3 hits in 79 CRISPR screens.
DR ChiTaRS; Kif1b; mouse.
DR PRO; PR:Q60575; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60575; Protein.
DR Bgee; ENSMUSG00000063077; Expressed in pigmented layer of retina and 274 other cell types or tissues.
DR ExpressionAtlas; Q60575; baseline and differential.
DR Genevisible; Q60575; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; ISO:MGI.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IMP:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; NAS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1990778; P:protein localization to cell periphery; ISO:MGI.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0010970; P:transport along microtubule; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd22727; FHA_KIF1B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Microtubule;
KW Mitochondrion; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT CHAIN 2..1816
FT /note="Kinesin-like protein KIF1B"
FT /id="PRO_0000125408"
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 556..612
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1702..1799
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 270..350
FT /note="Interaction with KBP"
FT /evidence="ECO:0000250"
FT REGION 1522..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..386
FT /evidence="ECO:0000255"
FT COILED 470..502
FT /evidence="ECO:0000255"
FT COILED 668..737
FT /evidence="ECO:0000255"
FT COILED 841..869
FT /evidence="ECO:0000255"
FT COMPBIAS 1524..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT VAR_SEQ 289..294
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7528108, ECO:0000303|Ref.4"
FT /id="VSP_002862"
FT VAR_SEQ 394..434
FT /note="IDPLIDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTA -> T (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7528108, ECO:0000303|Ref.4"
FT /id="VSP_002863"
FT VAR_SEQ 707..1196
FT /note="YESKLQALQRQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQ
FT FTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPSEMEKTHED
FT RPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVASSAQDDSETTMTG
FT SDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFD
FT DEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVA
FT IVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSAAMTR
FT SGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLK
FT LGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQN
FT IAVEVTESFVDYIKTKPIVFEVFGH -> ADSDSGDDSDKRSCEESWKLITSLREKLPP
FT SKLQTIVKKCGLPSSGKKREPIKMYQIPQRRRLSKDSKWVTISDLKIQAVKEICYEVAL
FT NDFRHSRQEIEALAIVKMKELCAMYGKKDPNERDSWRAVARDVWDTVGVGDEKIEDMMV
FT TGKGGTDVDDLKVHIDKLEDILQEVKKQNNMKDEEIKVLRNKMLKMEKVLPLIGSQEQK
FT SQGSHKTKEPLVAGANSVSDNGVSKGESGELGKEERVSQLMNGDPAFRRGRLRWMRQEQ
FT IRFKNLQQQEITKQLRRQNVPHRFIPPENRKPRFPFKSNPKHRNSWSPGTHIIITEDEV
FT IELRIPKDEEGRKENKEESQEKVGRAASRDVQSAWGTRSQDHIQVSKQHISNQQPPPQL
FT RWRSNSLNNGQPKTTRCQATASSESLNSHSGHPTADLQTFQAKRHIHQHRQPYCNYNTG
FT GQVEGSTASCCQKQTDKPSHCNQFVTPPRMRRQFSAPNLKAGRETTV (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:7528108"
FT /id="VSP_002864"
FT VAR_SEQ 1197..1816
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7528108"
FT /id="VSP_002865"
FT CONFLICT 117
FT /note="G -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..523
FT /note="GGTL -> RGDI (in Ref. 1; BAA04503)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="P -> S (in Ref. 4; BAA75243)"
FT /evidence="ECO:0000305"
FT CONFLICT 1608..1609
FT /note="KL -> TW (in Ref. 3; AAD39438)"
FT /evidence="ECO:0000305"
FT CONFLICT 1612
FT /note="I -> V (in Ref. 3; AAD39438)"
FT /evidence="ECO:0000305"
FT CONFLICT 1784
FT /note="D -> G (in Ref. 4; BAA75243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1816 AA; 204081 MW; E316EC295138E5DE CRC64;
MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKQ DPETNLSTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKSKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI
NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLIDD YSGSGGKYLK DFQNNKHRYL
LASENQRPGN FSTASMGSLT SSPSSCSLNS QVGLTSVTSI QERIMSTPGG EEAIERLKES
EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED
PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CLFRSERSNT GEVIVTLEPC
ERSETYVNGK RVAHPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT
FAQRELLEKQ GIDMKQEMEK RLQEMEILYK KEKEEADLLL EQQRLDYESK LQALQRQVET
RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS
VELKKKVQFQ FVLLTDTLYS PVPPELLPSE MEKTHEDRPF PRTVVAVEVQ DLKNGATHYW
SLDKLKQRLD LMREMYDRAG EVASSAQDDS ETTMTGSDPF YDRFHWFKLV GSSPIFHGCV
NERLADRTPS PTFSTADSDI TELADEQQDA MEDFDDEAFV DDTGSDAGTE EGSELFSDGH
DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP
DYGSGIRQSG TAKISFDNEY FNQSDFSSAA MTRSGLSLEE LRIVEGQGQS SEVISPPEEV
NRMNDLDLKS GTLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF
NFLHRHDEAF STEPLKNNGR GSPLGFYHVQ NIAVEVTESF VDYIKTKPIV FEVFGHYQQH
PLHLQGQDLN SPPQPSRRFF PPPMPLSKPV PATKLNTMNK TTLGQSMSKY DLLVWFEISE
LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR
NKPEVDEAAV DAVLSLNIIS AKSLKAAHSS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK
IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRNLFGSGYS KSPDSNRVTG
IYELSLCKMA DTGSPGMQRR RRKVLDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE
LLHEVEKTRH FLLLRERLGD SVPKSLSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP
SESSGYDSAD VESLVDREKE LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS
VSSFSSSTLT PSSTCPSLVD SRSSSMDQKT PEANSRASSP CQEFEQFQIV PTVETPYLAR
AGKNEFLNLV PDIEEVRAGS VVSKKGYLHF KEPLSSNWAK HFVVVRRPYV FIYNSDKDPV
ERGIINLSTA QVEYSEDQQA MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG
TIRSKLSRRC PSQPKY
//
