DEN4C_MOUSE
ID DEN4C_MOUSE Reviewed; 1906 AA.
AC A6H8H2; A2AJX5; Q3U2K9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DENN domain-containing protein 4C;
GN Name=Dennd4c;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1264 (ISOFORM 2).
RC STRAIN=NOD;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-971, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740; THR-966; SER-971;
RP SER-987; SER-1096; SER-1248 AND SER-1637, AND IDENTIFICATION BY MASS
RP 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).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT SER-1043; SER-1096 AND SER-1321, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21454697; DOI=10.1074/jbc.c111.228908;
RA Sano H., Peck G.R., Kettenbach A.N., Gerber S.A., Lienhard G.E.;
RT "Insulin-stimulated GLUT4 protein translocation in adipocytes requires the
RT Rab10 guanine nucleotide exchange factor Dennd4C.";
RL J. Biol. Chem. 286:16541-16545(2011).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10.
CC Promotes the exchange of GDP to GTP, converting inactive GDP-bound
CC RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4
CC glucose transporter-enriched vesicles delivery to the plasma membrane
CC in response to insulin. {ECO:0000269|PubMed:21454697}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:21454697}. Cell membrane
CC {ECO:0000269|PubMed:21454697}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21454697}. Note=Associates with SLC2A4/GLUT4
CC storage vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6H8H2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6H8H2-2; Sequence=VSP_044491;
CC -!- PTM: Phosphorylated in response to insulin.
CC {ECO:0000269|PubMed:21454697}.
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DR EMBL; AL772228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146602; AAI46603.1; -; mRNA.
DR EMBL; AK155220; BAE33131.1; -; mRNA.
DR CCDS; CCDS51218.2; -. [A6H8H2-1]
DR RefSeq; NP_908976.1; NM_184088.1. [A6H8H2-1]
DR RefSeq; XP_006538085.1; XM_006538022.2. [A6H8H2-2]
DR RefSeq; XP_006538086.1; XM_006538023.3. [A6H8H2-2]
DR AlphaFoldDB; A6H8H2; -.
DR SMR; A6H8H2; -.
DR BioGRID; 236853; 5.
DR STRING; 10090.ENSMUSP00000080685; -.
DR iPTMnet; A6H8H2; -.
DR PhosphoSitePlus; A6H8H2; -.
DR EPD; A6H8H2; -.
DR jPOST; A6H8H2; -.
DR MaxQB; A6H8H2; -.
DR PaxDb; A6H8H2; -.
DR PRIDE; A6H8H2; -.
DR ProteomicsDB; 279619; -. [A6H8H2-1]
DR ProteomicsDB; 279620; -. [A6H8H2-2]
DR Antibodypedia; 10280; 83 antibodies from 18 providers.
DR Ensembl; ENSMUST00000082026; ENSMUSP00000080685; ENSMUSG00000038024. [A6H8H2-2]
DR Ensembl; ENSMUST00000142837; ENSMUSP00000123367; ENSMUSG00000038024. [A6H8H2-1]
DR GeneID; 329877; -.
DR KEGG; mmu:329877; -.
DR UCSC; uc008tmb.2; mouse. [A6H8H2-1]
DR UCSC; uc008tmc.1; mouse. [A6H8H2-2]
DR CTD; 55667; -.
DR MGI; MGI:1914769; Dennd4c.
DR VEuPathDB; HostDB:ENSMUSG00000038024; -.
DR eggNOG; KOG2127; Eukaryota.
DR GeneTree; ENSGT00940000158215; -.
DR InParanoid; A6H8H2; -.
DR OMA; TWESEHR; -.
DR OrthoDB; 75304at2759; -.
DR TreeFam; TF313237; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 329877; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dennd4c; mouse.
DR PRO; PR:A6H8H2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A6H8H2; protein.
DR Bgee; ENSMUSG00000038024; Expressed in stroma of bone marrow and 251 other tissues.
DR ExpressionAtlas; A6H8H2; baseline and differential.
DR Genevisible; A6H8H2; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030904; C:retromer complex; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS51498; MABP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1906
FT /note="DENN domain-containing protein 4C"
FT /id="PRO_0000420446"
FT DOMAIN 40..199
FT /note="MABP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT DOMAIN 191..363
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 384..520
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 522..640
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REPEAT 818..852
FT /note="PPR"
FT REGION 904..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 966
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 973
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21454697"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21454697,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21454697"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT MOD_RES 1637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZ89"
FT VAR_SEQ 910
FT /note="S -> SAPQNAACGSDGDTVSHGSVDSSNDANNGEHTVFVRDLISLDSIDNH
FT SST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044491"
SQ SEQUENCE 1906 AA; 211458 MW; 705904CB0F5BED64 CRC64;
MIEDKGPRVT DYFVVAGLTD TSTLLDQEIN RTDTNSIGPK APITDIAVII KSAGETVPEG
YTCVEATPSA LQANLNYGSL KSPELFLCYR RGRDKPPLTD IGVLYEGKER LMPGCEVIQA
TPYGRCANVN NSSTTSQRIF ITYRRAPPVR SQNSLAVTDI CVIITSKGET PPHTFCKVDK
NLNCGMWGSN VFLCYKKSVP ASNAIAYKAG LIFRYPEEDY ESFPLSPSVP LFCLPMGATI
ECWDPQIKYP LPVFSTFVLT GSSAEKVYGA AIQFYEPYSQ ERLTEKQLTQ LGLLTLVEKR
VVSKPINSNK CICLLSHWPF FEAFKNFLMF IYKVSVSGPH PLPIEKHISH FMQNIPFPSP
QRPRILIQLS VHDAFILSQP VSTPLPLSGA NFSSLLMNLG PENCATLLLL VLLESKILLH
SLRPAVLTGV AEAVVAMIFP FQWQCPYIPL CPLSLAGVLS APLPFIVGVD SRYFDLHDPP
QDVVCIDLDT NTLYVADERK NINWKQLPKR PCKSLLGTLR RLYQQLCSVH RKPQESSAIE
MTPIEADYSW QKKMTQLEME IQETFLRFMA SILKGYRSYL RPITEAPSNK ATAADSLFDR
QGFLKSRDRA YTKFYTLLSK TQIFIRFIEE CSFVSDKDTG LAFFDDCIEK LFPDKGVERT
EKVDLDSAED TRLIELDDSQ RSEHTVFIMP PEPPPDDGNN LSPQYSYTYF PRLDLKLFDS
PQKLKLCFNR HPPGSSITNS PALMAKRTKQ EIKTAHKLAK RCYTNPPQWA KYLFSHCYSL
WFICLPAYVR VSHPKVRALQ QAHDVLVKMR KTDVDPLDEV CYRVVMQLCG LWVNPVLAVR
VLFEMKTARI KPNAITYGYY NKVVLESPWP SSTRSGIFLW TKVRNVVHGL AQFRQPLKKT
GQKSQVFSIS GGQSDQGYGS KDELVKEGAD GHAPEEHTPP ELTTTELHIE EECDISAIVS
KHLQPTPEPQ SPTEPPAWGS SIVKVPSGLF DTNNRTSTGS TSTVLFSTQA PVEDAVFSEV
TNFKKNGDRG EKKQKHFPER SCSFSSESRA GMLLKKSSLD LNSSEMAIMM GADAKILTAA
LTCPKTSPPH VTRTHSFENV NCHLADSRTR MSEGTRDSEH RSSPVLEMLE ESQELLEPVV
GDNVAETAAE MTCNSLQSNS HSDQSRDTQA GAQDPVNKRS SSYATRKAIE REDVETGLDP
LSLLATECVE KTSDSEDKLF SPVISRNLAD EIESYMNLKS PLGSKSCSME LHGEGNQEPG
SPAVFAHPLE RSSSLPSDRG PPARDSTETE KSSPAVSSSK TLTGRFKPQS PYRAYKDRST
SLSALVRSSP NSSLGSVVNS LSGLKLDNIL SGPKIDVLKS SMKQAATVAS KMWVAVASAY
SYSDDEEETN KDYSFPAGLE DHHIVGETLS PNTSVSGLVP SELTQSNTSL GSSSSSGDVG
KLQCPAGEVP FSRNIKGQDF EKSDHGSSQN TSMSSIYQNC AMEVLMSSCS QCRACGALVY
DEEIMAGWTA DDSNLNTTCP FCKSNFLPLL NVEFKDLRGS ASFFLKPSTS GDSLQSGSIP
SASEPSEHKP TSSSAEPDLI SFMDFSKHSE TITEEASYTV ESSDEIKKTN GDVQSVKMSS
VPNSLSKRNV SLTRSHSVGG PLQNIDFSQR PFHGVSTVSL PSSLQEDVDH LGKRPSPPPV
SVPYLSPLVL RKELESLLEN EGDQVIHTSS FINQHPIIFW NLVWYFRRLD LPSNLPGLIL
TSEHCNGGVQ LPLSSLSQDS KLVYIQLLWD NINLHQEPGE PLYVSWRNLN SEKKPSLLSE
QQQAASALVE TIRQSIQQND VLKPINLLSQ QMKPGTKRQR SLYREILFLS LVSLGRENID
IEAFDNEYGL AYRSLPSESL ERLQRIDAPP SISVEWCRKC FGAPLI
