NSMF_MOUSE
ID NSMF_MOUSE Reviewed; 532 AA.
AC Q99NF2; A2AJ93; A2AJ94; Q8BPT0; Q8C9R5; Q9DBF4; Q9ERZ1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=NMDA receptor synaptonuclear signaling and neuronal migration factor;
DE AltName: Full=Juxtasynaptic attractor of caldendrin on dendritic boutons protein;
DE Short=Jacob protein;
DE AltName: Full=Nasal embryonic luteinizing hormone-releasing hormone factor;
DE Short=Nasal embryonic LHRH factor;
GN Name=Nsmf; Synonyms=Jac, Nelf;
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), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=NIH Swiss;
RX PubMed=10898796;
RA Kramer P.R., Wray S.;
RT "Novel gene expressed in nasal region influences outgrowth of olfactory
RT axons and migration of luteinizing hormone-releasing hormone (LHRH)
RT neurons.";
RL Genes Dev. 14:1824-1834(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Dieterich D.C., Hoffmann B., Seidenbecher C.I., Kreutz M.R.;
RT "Characterization of the novel brain-specific protein Jacob.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=15018815; DOI=10.1016/s1567-133x(01)00004-7;
RA Kramer P.R., Wray S.;
RT "Nasal embryonic LHRH factor (NELF) expression within the CNS and PNS of
RT the rodent.";
RL Gene Expr. Patterns 1:23-26(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [8]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=20025934; DOI=10.1016/j.mce.2009.11.016;
RA Xu N., Bhagavath B., Kim H.G., Halvorson L., Podolsky R.S., Chorich L.P.,
RA Prasad P., Xiong W.C., Cameron R.S., Layman L.C.;
RT "NELF is a nuclear protein involved in hypothalamic GnRH neuronal
RT migration.";
RL Mol. Cell. Endocrinol. 319:47-55(2010).
CC -!- FUNCTION: Couples NMDA-sensitive glutamate receptor signaling to the
CC nucleus and triggers long-lasting changes in the cytoarchitecture of
CC dendrites and spine synapse processes. Part of the cAMP response
CC element-binding protein (CREB) shut-off signaling pathway. Stimulates
CC outgrowth of olfactory axons and migration of gonadotropin-releasing
CC hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH)
CC neuronal cells. {ECO:0000269|PubMed:10898796}.
CC -!- SUBUNIT: Interacts with KPNA1; the interaction occurs in a calcium-
CC independent manner after synaptic NMDA receptor stimulation and is
CC required for nuclear import of NSMF but is competed by CABP1. Interacts
CC (via the central NLS-containing motif region) with CABP1 (via EF-hands
CC 1 and 2); the interaction occurs in a calcium-dependent manner after
CC synaptic NMDA receptor stimulation and prevents the nuclear import of
CC NSMF. Cannot be competed by calmodulin (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q99NF2-1; O88751-1: Cabp1; Xeno; NbExp=2; IntAct=EBI-15688721, EBI-15688755;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus envelope {ECO:0000250}. Nucleus
CC membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm.
CC Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane; Peripheral membrane protein. Cell
CC projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane
CC {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone-
CC releasing hormone (LHRH) cell membrane and axons projecting from the
CC olfactory pit and epithelium. Associates with transcriptionally active
CC chromatin regions. Detected at the nuclear membranes of CA1 neurons.
CC Cortical cytoskeleton. Localized in proximal apical dendrites.
CC Colocalizes with CABP1 in dendrites and dendritic spines.
CC Myristoylation is a prerequisite for extranuclear localization.
CC Translocates from dendrites to the nucleus during NMDA receptor-
CC dependent long-term potentiation (LTP) induction of synaptic
CC transmission at Schaffer collateral/CA1 synapses of hippocampal primary
CC neurons and in an importin-dependent manner (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q99NF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99NF2-2; Sequence=VSP_014767;
CC Name=3;
CC IsoId=Q99NF2-3; Sequence=VSP_014768;
CC Name=4;
CC IsoId=Q99NF2-4; Sequence=VSP_014764, VSP_014767, VSP_014769;
CC Name=5;
CC IsoId=Q99NF2-5; Sequence=VSP_014765, VSP_014766;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in immature migratory, in
CC comparison to postmigrating, gonadotropin-releasing hormone (GnRH)
CC neuronal cell lines (at protein level). Expressed in adult brain and
CC liver. In the brain, expressed in the primary pituitary gland, cortex,
CC hippocampus, olfactory bulb and thalamus. {ECO:0000269|PubMed:10898796,
CC ECO:0000269|PubMed:15018815, ECO:0000269|PubMed:20025934}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc embryo found at high levels within the
CC forebrain, olfactory epithelium and olfactory pit. At 12.5 dpc embryo
CC detected on olfactory axons including olfactory pathway on which the
CC LHRH neurons move. From 11.5 dpc to 17.5 dpc embryos expressed in LHRH
CC (luteinizing hormone-releasing hormone) neurons as they migrate from
CC the olfactory pit into the developing forebrain.
CC {ECO:0000269|PubMed:10898796}.
CC -!- INDUCTION: Up-regulated by gonadotropin releasing hormone (GnRH).
CC {ECO:0000269|PubMed:20025934}.
CC -!- PTM: Proteolytically processed after NMDA receptor activation. Cleaved
CC in a calcium-dependent and calpain-sensitive manner. Calpain cleavage
CC is essential for the translocation process from dendrites to the
CC nucleus (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Transport from dendrites to the nucleus is induced by
CC NMDA receptor activation and results in a rapid stripping of synaptic
CC contacts and a reduction of dendritic complexity (By similarity). KIF5C
CC associates to its 3'-UTR mRNA in granules along dendritic shafts,
CC suggesting that this protein may regulate its dendritic trafficking and
CC local translation at postsynaptic sites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NSMF family. {ECO:0000305}.
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DR EMBL; AF266508; AAF74501.2; -; mRNA.
DR EMBL; AJ278902; CAC27332.1; -; mRNA.
DR EMBL; AK004986; BAB23721.1; -; mRNA.
DR EMBL; AK019560; BAC25597.1; -; mRNA.
DR EMBL; AK041478; BAC30955.1; -; mRNA.
DR EMBL; AK045384; BAC32338.1; -; mRNA.
DR EMBL; AK053402; BAC35375.1; -; mRNA.
DR EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006642; AAH06642.1; -; mRNA.
DR CCDS; CCDS15745.1; -. [Q99NF2-1]
DR CCDS; CCDS15746.1; -. [Q99NF2-2]
DR CCDS; CCDS15747.1; -. [Q99NF2-3]
DR RefSeq; NP_001034475.1; NM_001039386.1. [Q99NF2-1]
DR RefSeq; NP_001034476.1; NM_001039387.1. [Q99NF2-2]
DR RefSeq; NP_001171125.1; NM_001177654.1.
DR RefSeq; NP_001171126.1; NM_001177655.1.
DR RefSeq; NP_064672.2; NM_020276.3. [Q99NF2-3]
DR AlphaFoldDB; Q99NF2; -.
DR SMR; Q99NF2; -.
DR IntAct; Q99NF2; 3.
DR STRING; 10090.ENSMUSP00000097908; -.
DR iPTMnet; Q99NF2; -.
DR PhosphoSitePlus; Q99NF2; -.
DR MaxQB; Q99NF2; -.
DR PaxDb; Q99NF2; -.
DR PRIDE; Q99NF2; -.
DR ProteomicsDB; 293985; -. [Q99NF2-1]
DR ProteomicsDB; 293986; -. [Q99NF2-2]
DR ProteomicsDB; 293987; -. [Q99NF2-3]
DR ProteomicsDB; 293988; -. [Q99NF2-4]
DR ProteomicsDB; 293989; -. [Q99NF2-5]
DR Antibodypedia; 32451; 176 antibodies from 27 providers.
DR DNASU; 56876; -.
DR Ensembl; ENSMUST00000006646; ENSMUSP00000006646; ENSMUSG00000006476. [Q99NF2-2]
DR Ensembl; ENSMUST00000100334; ENSMUSP00000097908; ENSMUSG00000006476. [Q99NF2-1]
DR Ensembl; ENSMUST00000102931; ENSMUSP00000099995; ENSMUSG00000006476. [Q99NF2-3]
DR GeneID; 56876; -.
DR KEGG; mmu:56876; -.
DR UCSC; uc008iqa.1; mouse. [Q99NF2-5]
DR UCSC; uc008iqb.1; mouse. [Q99NF2-1]
DR UCSC; uc008iqc.1; mouse. [Q99NF2-2]
DR UCSC; uc008iqd.1; mouse. [Q99NF2-3]
DR CTD; 26012; -.
DR MGI; MGI:1861755; Nsmf.
DR VEuPathDB; HostDB:ENSMUSG00000006476; -.
DR eggNOG; ENOG502QRME; Eukaryota.
DR GeneTree; ENSGT00390000000459; -.
DR HOGENOM; CLU_038476_2_0_1; -.
DR InParanoid; Q99NF2; -.
DR OMA; RQGSREC; -.
DR OrthoDB; 611342at2759; -.
DR PhylomeDB; Q99NF2; -.
DR TreeFam; TF331286; -.
DR BioGRID-ORCS; 56876; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Nsmf; mouse.
DR PRO; PR:Q99NF2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99NF2; protein.
DR Bgee; ENSMUSG00000006476; Expressed in medial dorsal nucleus of thalamus and 242 other tissues.
DR ExpressionAtlas; Q99NF2; baseline and differential.
DR Genevisible; Q99NF2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISS:UniProtKB.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
DR InterPro; IPR033374; NSMF.
DR PANTHER; PTHR32061; PTHR32061; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Lipoprotein; Membrane; Myristate; Nucleus; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..532
FT /note="NMDA receptor synaptonuclear signaling and neuronal
FT migration factor"
FT /id="PRO_0000096779"
FT REGION 2..235
FT /note="Necessary and sufficient to elicit dendritic
FT processes and synaptic contacts"
FT /evidence="ECO:0000250"
FT REGION 34..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 249..252
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 141..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPI6"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPI6"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MRGAPVTM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014764"
FT VAR_SEQ 212..226
FT /note="DDVPIRTWFPKENLF -> GEGLIFGPGQIPAGL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014765"
FT VAR_SEQ 227..532
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014766"
FT VAR_SEQ 238..239
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014767"
FT VAR_SEQ 240..262
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10898796"
FT /id="VSP_014768"
FT VAR_SEQ 280..309
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014769"
FT CONFLICT 248
FT /note="K -> N (in Ref. 3; BAC35375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 60293 MW; DE83212A82B90987 CRC64;
MGAAASRRRA LRSEAMSSVA AKVRAARAFG EYLSQSHPEN RNGADHLLAD AYSGHDGSPE
MQPAPQNKRR LSLVSNGRYE GSISDEAVSG KPAIEGPQPH VYTISREPAL LPGSEAEAIE
LAVVKGRRQR ERHPHHHSQP LRASPGSSRE DISRPCQSWA GSRQGSKECP GCAQLVPGPS
SRAFGLEQPP LPEAPGRHKK LERMYSVDGV SDDVPIRTWF PKENLFSFQT ATTTMQAISV
FRGYAERKRR KRENDSASVI QRNFRKHLRM VGSRRVKAQT FAERRERSFS RSWSDPTPMK
ADTSHDSRDS SDLQSSHCTL DEACEDLDWD TEKGLEAMAC NTEGFLPPKV MLISSKVPKA
EYIPTIIRRD DPSIIPILYD HEHATFEDIL EEIEKKLNIY HKGAKIWKML IFCQGGPGHL
YLLKNKVATF AKVEKEEDMI HFWKRLSRLM SKVNPEPNVI HIMGCYILGN PNGEKLFQNL
RTLMTPYKVT FESPLELSAQ GKQMIETYFD FRLYRLWKSR QHSKLLDFDD VL
