NCDN_MOUSE
ID NCDN_MOUSE Reviewed; 729 AA.
AC Q9Z0E0; Q3TCW4; Q80TW1; Q91YH7; Q9CW81; Q9QUQ0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Neurochondrin;
DE AltName: Full=M-Sema F-associating protein of 75 kDa;
DE AltName: Full=Norbin;
GN Name=Ncdn; Synonyms=Kiaa0607, Sfap75;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RC STRAIN=C57BL/6N;
RX PubMed=10231559; DOI=10.1016/s0167-4889(99)00039-7;
RA Ishiduka Y., Mochizuki R., Yanai K., Takatsuka M., Nonomura T., Niida S.,
RA Horiguchi H., Maeda N., Fukamizu A.;
RT "Induction of hydroxyapatite resorptive activity in bone marrow cell
RT populations resistant to bafilomycin A1 by a factor with restricted
RT expression to bone and brain, neurochondrin.";
RL Biochim. Biophys. Acta 1450:92-98(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain;
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]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-729.
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SEMA4C.
RX PubMed=11162505; DOI=10.1006/bbrc.2000.4080;
RA Ohoka Y., Hirotani M., Sugimoto H., Fujioka S., Furuyama T., Inagaki S.;
RT "Semaphorin 4C, a transmembrane semaphorin, associates with a neurite-
RT outgrowth-related protein, SFAP75.";
RL Biochem. Biophys. Res. Commun. 280:237-243(2001).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11445285; DOI=10.1016/s0304-3940(01)01981-4;
RA Mani S.T., Kumar R.C., Thakur M.K.;
RT "Age- and sex-related expression of norbin in the brain cortex of mice.";
RL Neurosci. Lett. 308:57-59(2001).
RN [8]
RP ERRATUM OF PUBMED:11445285.
RA Ohoka Y., Hirotani M., Sugimoto H., Fujioka S., Furuyama T., Inagaki S.;
RL Biochem. Biophys. Res. Commun. 281:266-266(2001).
RN [9]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=14559245; DOI=10.1016/j.bbrc.2003.09.153;
RA Mochizuki R., Dateki M., Yanai K., Ishizuka Y., Amizuka N., Kawashima H.,
RA Koga Y., Ozawa H., Fukamizu A.;
RT "Targeted disruption of the neurochondrin/norbin gene results in embryonic
RT lethality.";
RL Biochem. Biophys. Res. Commun. 310:1219-1226(2003).
RN [10]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15007648; DOI=10.1007/s00427-004-0396-2;
RA Istvanffy R., Vogt Weisenhorn D.M., Floss T., Wurst W.;
RT "Expression of neurochondrin in the developing and adult mouse brain.";
RL Dev. Genes Evol. 214:206-209(2004).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15790563; DOI=10.1074/jbc.m414033200;
RA Dateki M., Horii T., Kasuya Y., Mochizuki R., Nagao Y., Ishida J.,
RA Sugiyama F., Tanimoto K., Yagami K., Imai H., Fukamizu A.;
RT "Neurochondrin negatively regulates CaMKII phosphorylation, and nervous
RT system-specific gene disruption results in epileptic seizure.";
RL J. Biol. Chem. 280:20503-20508(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH DIAPH1.
RX PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA Schwaibold E.M., Brandt D.T.;
RT "Identification of Neurochondrin as a new interaction partner of the FH3
RT domain of the Diaphanous-related formin Dia1.";
RL Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20007903; DOI=10.1126/science.1178496;
RA Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H.,
RA Nestler E., Aperia A., Flajolet M., Greengard P.;
RT "Norbin is an endogenous regulator of metabotropic glutamate receptor 5
RT signaling.";
RL Science 326:1554-1557(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, 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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-75, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probably involved in signal transduction, in the nervous
CC system, via increasing cell surface localization of GRM5 and positively
CC regulating its signaling. Required for the spatial learning process.
CC Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein
CC kinase 2 (CaMK2) phosphorylation. May play a role in modulating
CC melanin-concentrating hormone-mediated functions via its interaction
CC with MCHR1 that interferes with G protein-coupled signal transduction.
CC May be involved in bone metabolism. May also be involved in neurite
CC outgrowth. {ECO:0000269|PubMed:15790563, ECO:0000269|PubMed:18572016,
CC ECO:0000269|PubMed:20007903}.
CC -!- SUBUNIT: Interacts with MCHR1 (By similarity). Interacts with SEMA4C
CC (PubMed:11162505). Interacts with DIAPH1 (via FH3 domain)
CC (PubMed:18572016). Interacts with GRM5 (By similarity).
CC {ECO:0000250|UniProtKB:O35095, ECO:0000250|UniProtKB:Q9UBB6,
CC ECO:0000269|PubMed:11162505, ECO:0000269|PubMed:18572016}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O35095}. Endosome membrane
CC {ECO:0000250|UniProtKB:O35095}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O35095}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O35095}. Postsynapse
CC {ECO:0000250|UniProtKB:O35095}. Note=Localizes to somatic regions of
CC neurons. Localization to endosome membrane requires palmitoylation.
CC {ECO:0000250|UniProtKB:O35095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Neurochondrin-1;
CC IsoId=Q9Z0E0-1; Sequence=Displayed;
CC Name=2; Synonyms=Neurochondrin-2;
CC IsoId=Q9Z0E0-2; Sequence=VSP_032317;
CC -!- TISSUE SPECIFICITY: Expressed in the neuronal, chondral and bone
CC tissues. Expressed in dendrites. Enriched in the brain in the surface
CC layer I-IV. In brains, protein level increases in male but decreases in
CC female with advancing age (at protein level). In adult brains, it is
CC highly expressed in the forebrain and hindbrain. Highly expressed in
CC the hippocampus, piriform cortex, septum, amygdaloid complex, medial
CC geniculate nucleus, inferior colliculus, cerebellar nuclei and the
CC nuclei of the Vth, VIIth, and XIIth cranial nerves. In bone tissues, it
CC is expressed in osteoblasts and osteocytes.
CC {ECO:0000269|PubMed:11162505, ECO:0000269|PubMed:11445285,
CC ECO:0000269|PubMed:15007648, ECO:0000269|PubMed:20007903}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, it is first expressed in
CC the hindbrain and spinal cord at 10.5 dpc followed by expression in the
CC midbrain at 11.5 dpc. By 18 dpc it is also expressed in the
CC diencephalon and telencephalon, with a strongest expression in the
CC hindbrain. Highly expressed in the developing olfactory bulb and in the
CC lateral choroid plexus. {ECO:0000269|PubMed:11445285,
CC ECO:0000269|PubMed:14559245, ECO:0000269|PubMed:15007648}.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC1, ZDHHC3 and ZDHHC11
CC regulates the association of NCDN with endosome membranes. May also be
CC palmitoylated by ZDHHC7. {ECO:0000250|UniProtKB:O35095}.
CC -!- DISRUPTION PHENOTYPE: Death between 3.5 and 6.5 dpc. Heterozygous
CC mutant do not display gross anatomic abnormalities. They however show
CC abnormalities in developing cartilage. Nervous system-specific gene
CC disruption by conditional knockout results in epileptic seizure.
CC Displays no overt neurite outgrowth phenotype (PubMed:15790563). Shows
CC a behavioral phenotype associated with a rodent model of schizophrenia,
CC as observed in alterations in both sensorimotor gating and
CC psychotomimetic-induced locomotor activity.
CC {ECO:0000269|PubMed:14559245, ECO:0000269|PubMed:15790563,
CC ECO:0000269|PubMed:20007903}.
CC -!- SIMILARITY: Belongs to the neurochondrin family. {ECO:0000305}.
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DR EMBL; AB017608; BAA75226.1; -; Genomic_DNA.
DR EMBL; AB017609; BAA75227.1; -; Genomic_DNA.
DR EMBL; AB019041; BAA75228.1; -; Genomic_DNA.
DR EMBL; AB019041; BAA75229.1; -; Genomic_DNA.
DR EMBL; AK002938; BAB22468.2; -; mRNA.
DR EMBL; AK154889; BAE32905.1; -; mRNA.
DR EMBL; AK170502; BAE41841.1; -; mRNA.
DR EMBL; AL606908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017126; AAH17126.1; -; mRNA.
DR EMBL; AK122327; BAC65609.1; -; mRNA.
DR CCDS; CCDS18659.1; -. [Q9Z0E0-1]
DR RefSeq; NP_036116.3; NM_011986.4. [Q9Z0E0-1]
DR RefSeq; XP_006503181.1; XM_006503118.3.
DR RefSeq; XP_006503182.1; XM_006503119.3.
DR AlphaFoldDB; Q9Z0E0; -.
DR SMR; Q9Z0E0; -.
DR BioGRID; 205020; 14.
DR IntAct; Q9Z0E0; 10.
DR MINT; Q9Z0E0; -.
DR STRING; 10090.ENSMUSP00000030637; -.
DR iPTMnet; Q9Z0E0; -.
DR PhosphoSitePlus; Q9Z0E0; -.
DR SwissPalm; Q9Z0E0; -.
DR EPD; Q9Z0E0; -.
DR MaxQB; Q9Z0E0; -.
DR PaxDb; Q9Z0E0; -.
DR PeptideAtlas; Q9Z0E0; -.
DR PRIDE; Q9Z0E0; -.
DR ProteomicsDB; 252789; -. [Q9Z0E0-1]
DR ProteomicsDB; 252790; -. [Q9Z0E0-2]
DR Antibodypedia; 17311; 215 antibodies from 28 providers.
DR DNASU; 26562; -.
DR Ensembl; ENSMUST00000030637; ENSMUSP00000030637; ENSMUSG00000028833. [Q9Z0E0-1]
DR Ensembl; ENSMUST00000106116; ENSMUSP00000101722; ENSMUSG00000028833. [Q9Z0E0-1]
DR GeneID; 26562; -.
DR KEGG; mmu:26562; -.
DR UCSC; uc008utt.2; mouse. [Q9Z0E0-1]
DR CTD; 23154; -.
DR MGI; MGI:1347351; Ncdn.
DR VEuPathDB; HostDB:ENSMUSG00000028833; -.
DR eggNOG; KOG2611; Eukaryota.
DR GeneTree; ENSGT00390000013601; -.
DR HOGENOM; CLU_012443_0_0_1; -.
DR InParanoid; Q9Z0E0; -.
DR OMA; DRKYELC; -.
DR OrthoDB; 311670at2759; -.
DR PhylomeDB; Q9Z0E0; -.
DR TreeFam; TF323752; -.
DR BioGRID-ORCS; 26562; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Ncdn; mouse.
DR PRO; PR:Q9Z0E0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z0E0; protein.
DR Bgee; ENSMUSG00000028833; Expressed in CA3 field of hippocampus and 242 other tissues.
DR Genevisible; Q9Z0E0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0045453; P:bone resorption; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008709; Neurochondrin.
DR PANTHER; PTHR13109; PTHR13109; 1.
DR Pfam; PF05536; Neurochondrin; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm; Endosome;
KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein;
KW Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT CHAIN 2..729
FT /note="Neurochondrin"
FT /id="PRO_0000324618"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB6"
FT MOD_RES 75
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35095"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O35095"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O35095"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032317"
FT CONFLICT 109
FT /note="A -> S (in Ref. 5; AAH17126)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="G -> D (in Ref. 3; BAE41841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 78895 MW; F23C439BDE1EDD9C CRC64;
MSCCDLAAAG QLGKAGIMAS DCEPALNQAE SRNPTLERYL GALREAKNDS EQFAALLLVT
KAVKAGDIDA KTRRRIFDAV GFTFPNRLLT TKEAPDGCPD HVLRALGVAL LACFCSDPEL
ASHPQVLNKI PILSTFLTAR GDPDDAARRS MIDDTYQCLT AVAGTPRGPR HLIAGGTVSA
LCQAYLGHGY GFDQALALLV GLLAAAETQC WKEAEPDLLA VLRGLSEDFQ RAEDASKFEL
CQLLPLFLPP TTVPPECHRD LQAGLARILG SKLSSWQRNP ALKLAARLAH ACGSDWIPVG
SSGSKFLALL VNLACVEVRL ALEETGTEVK EDVVTACYAL MELGIQECTR CEQSLLKEPQ
KVQLVSIMKE AIGAVIHYLL QVGPEKQKEP FVFASVRILG AWLAEETSSL RKEVCQLLPF
LVRYAKTLYE EAEEASDISQ QVANLAISPT TPGPSWPGDA LRLLLPGWCH LTVEDGPREI
LIKEGAPSLL CKYFLQQWEL TSPGHDTSVL PDSVEIGLQT CCHIFLNLVV TAPGLIKRDA
CFTSLMNTLM TSLPSLVQQQ GRLLLAANVA TLGLLMARLL STSPALQGTP ASRGFFAAAI
LFLSQSHVAR ATPGSDQAVL ALSPDYEGIW ADLQELWFLG MQAFTGCVPL LPWLAPAALR
SRWPQELLQL LGSVSPNSVK PEMVAAYQGV LVELARANRL CREAMRLQAG EETASHYRMA
ALEQCLSEP
