CUL7_MOUSE
ID CUL7_MOUSE Reviewed; 1689 AA.
AC Q8VE73; Q3UHY3; Q497I2; Q6A0D6; Q6PB63; Q8R3W4; Q9CVD5;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cullin-7;
DE Short=CUL-7;
DE AltName: Full=p185;
DE AltName: Full=p193;
GN Name=Cul7; Synonyms=Kiaa0076;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-1689 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1689 (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Jaw, Limb, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-1689 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12904573; DOI=10.1073/pnas.1733908100;
RA Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.;
RT "Targeted disruption of p185/Cul7 gene results in abnormal vascular
RT morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003).
RN [6]
RP INTERACTION WITH CUL1 AND FBXW8.
RX PubMed=16880526; DOI=10.1128/mcb.00595-06;
RA Tsunematsu R., Nishiyama M., Kotoshiba S., Saiga T., Kamura T.,
RA Nakayama K.I.;
RT "Fbxw8 is essential for Cul1-Cul7 complex formation and for placental
RT development.";
RL Mol. Cell. Biol. 26:6157-6169(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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: Core component of the 3M and Cul7-RING(FBXW8) complexes,
CC which mediates the ubiquitination of target proteins. Core component of
CC the 3M complex, a complex required to regulate microtubule dynamics and
CC genome integrity. It is unclear how the 3M complex regulates
CC microtubules, it could act by controlling the level of a microtubule
CC stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity
CC and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-
CC protein ligase with FBXW8, which mediates ubiquitination and consequent
CC degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1.
CC Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite
CC patterning in brain. Mediates ubiquitination and degradation of IRS1 in
CC a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and
CC binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2).
CC The Cul7-RING(FBXW8) complex also mediates ubiquitination of
CC MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1,
CC leading to its degradation, thereby affecting cell proliferation and
CC differentiation. Acts as a regulator in trophoblast cell epithelial-
CC mesenchymal transition and placental development. Does not promote
CC polyubiquitination and proteasomal degradation of p53/TP53. While the
CC Cul7-RING(FBXW8) and the 3M complexes are associated and involved in
CC common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have
CC additional functions (By similarity). Probably plays a role in the
CC degradation of proteins involved in endothelial proliferation and/or
CC differentiation. {ECO:0000250, ECO:0000269|PubMed:12904573}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7,
CC CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1,
CC SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not
CC with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity.
CC Interacts with FBXW8; interaction is mutually exclusive of binding to
CC CUL9 or p53/TP53. Interacts with p53/TP53; the interaction
CC preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9
CC heterodimer seems to interact specifically with p53/TP53. Interacts
CC with OBSL1 (By similarity). Interacts with CUL1; the interactions seems
CC to be mediated by FBXW8. Interacts (as part of the 3M complex) with
CC HDAC4 and HDAC5; it is negatively regulated by ANKRA2 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16880526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons;
CC localization to Golgi is mediated by OBSL1. During mitosis, localizes
CC to the mitotic apparatus. CCDC8 is required for centrosomal location
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VE73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VE73-3; Sequence=VSP_038331;
CC -!- DISRUPTION PHENOTYPE: Mice are neonatal lethal and show vascular
CC defects in both the embryo and the placenta.
CC {ECO:0000269|PubMed:12904573}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AK008655; BAB25811.1; -; mRNA.
DR EMBL; AK147156; BAE27723.1; -; mRNA.
DR EMBL; CT030702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019645; AAH19645.1; -; mRNA.
DR EMBL; BC026946; AAH26946.2; -; mRNA.
DR EMBL; BC059865; AAH59865.1; -; mRNA.
DR EMBL; BC100544; AAI00545.1; -; mRNA.
DR EMBL; AK172882; BAD32160.1; -; mRNA.
DR CCDS; CCDS28833.1; -. [Q8VE73-1]
DR RefSeq; NP_079887.3; NM_025611.5. [Q8VE73-1]
DR AlphaFoldDB; Q8VE73; -.
DR SMR; Q8VE73; -.
DR BioGRID; 211530; 13.
DR CORUM; Q8VE73; -.
DR STRING; 10090.ENSMUSP00000049128; -.
DR iPTMnet; Q8VE73; -.
DR PhosphoSitePlus; Q8VE73; -.
DR MaxQB; Q8VE73; -.
DR PaxDb; Q8VE73; -.
DR PRIDE; Q8VE73; -.
DR ProteomicsDB; 285435; -. [Q8VE73-1]
DR ProteomicsDB; 285436; -. [Q8VE73-3]
DR Antibodypedia; 4223; 207 antibodies from 37 providers.
DR DNASU; 66515; -.
DR Ensembl; ENSMUST00000043464; ENSMUSP00000049128; ENSMUSG00000038545. [Q8VE73-1]
DR GeneID; 66515; -.
DR KEGG; mmu:66515; -.
DR UCSC; uc008ctp.1; mouse. [Q8VE73-1]
DR CTD; 9820; -.
DR MGI; MGI:1913765; Cul7.
DR VEuPathDB; HostDB:ENSMUSG00000038545; -.
DR eggNOG; ENOG502RDJD; Eukaryota.
DR GeneTree; ENSGT00940000153954; -.
DR HOGENOM; CLU_001067_1_0_1; -.
DR InParanoid; Q8VE73; -.
DR OMA; NCLVVRI; -.
DR PhylomeDB; Q8VE73; -.
DR TreeFam; TF101154; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66515; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cul7; mouse.
DR PRO; PR:Q8VE73; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VE73; protein.
DR Bgee; ENSMUSG00000038545; Expressed in saccule of membranous labyrinth and 243 other tissues.
DR ExpressionAtlas; Q8VE73; baseline and differential.
DR Genevisible; Q8VE73; MM.
DR GO; GO:1990393; C:3M complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0045601; P:regulation of endothelial cell differentiation; NAS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR031223; CUL7.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR22771:SF3; PTHR22771:SF3; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..1689
FT /note="Cullin-7"
FT /id="PRO_0000119803"
FT DOMAIN 793..972
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT REGION 349..449
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250"
FT REGION 1321..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 1567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038331"
FT CONFLICT 395
FT /note="G -> V (in Ref. 1; BAE27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="D -> E (in Ref. 4; BAD32160)"
FT /evidence="ECO:0000305"
FT CONFLICT 777..779
FT /note="IQM -> DAW (in Ref. 3; AAH19645)"
FT /evidence="ECO:0000305"
FT CONFLICT 855..922
FT /note="Missing (in Ref. 3; AAH59865)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="G -> R (in Ref. 1; BAE27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="Q -> E (in Ref. 3; AAH59865)"
FT /evidence="ECO:0000305"
FT CONFLICT 1482
FT /note="S -> L (in Ref. 1; BAB25811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1495
FT /note="P -> L (in Ref. 1; BAB25811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1689 AA; 192292 MW; 6ED4641B577E53CD CRC64;
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHNGHPEYQI RWLILRRGDD GDRDSTVDCK
AEHILLWMSD DEIYANCHKM LGENGQVIAP SRESTEAGAL DKSVLGEMET DVKSLIQRAL
RQLEECVGTV PPAPLLHTVH VLSAYASIEP LTGIFKDRRV VNLLMHMLSS PDYQIRWSAG
RMIQALSSHD AGTRTQILLS LSQQEAIEKH LDFDSRCALL ALFAQATLTE HPMSFEGVQL
PQVPGRLLFS LVKRYLHVTF LLDRLNGDAG DQGAQNNFIP EELNVGRGRL ELEFSMAMGT
LISELVQAMR WDGASSRPES SSSSTFQPRP AQFRPYTQRF RRSRRFRPRA SFASFNTYAL
YVRDTLRPGM RVRMLENYEE IAAGDEGQFR QSNDGVPPAQ VLWDSTGHTY WVHWHMLEIL
GFEEDIEDVI DIEELQELGA NGALSIVPPS QRWKPITQLF AEPYVVPEEE DREESENLTQ
AEWWELLFFI RQLSEAERLH IVDLLQDHLE EERVLDYDML PELTVPVDLA QDLLLSLPQQ
LEDSALRDLF SCSVYRKYGP EVLVGHLSYP FVPGAQPNLF GANEESEAKD PPLQSASPAL
QRLVESLGPE GEVLVELEQA LGSEAPQETE VKSCLLQLQE QPQPFLALMR SLDTSASNKT
LHLTVLRILM QLVNFPEALL LPWHEAMDAC VTCLRSPNTD REVLQELIFF LHRLTTTSRD
YAVILNQLGA RDAISKVLEK HRGKLELAQE LRDMVSKCEK HAHLYRKLTT NILGGCIQMV
LGQIEDHRRT HRPIQIPFFD VFLRYLCQGS SEEMKKNRYW EKVEVSSNPQ RASRLTDRNP
KTYWESSGRA GSHFITLHMR PGVIIRQLTL LVAGEDSSYM PAWVVVCGGN SIKSVNKELN
TVNVMPSASR VTLLENLTRF WPIIQIRIKR CQQGGINTRI RGLEVLGPKP TFWPVFREQL
CRHTRLFYMV RAQAWSQDIA EDRRSLLHLS SRLNGALRHE QNFAERFLPD MEAAQALSKT
CWEALVSPLV QNITSPDEDS TSSLGWLLDQ YLGCREAAYN PQSRAAAFSS RVRRLTHLLV
HVEPREAAPP VVAIPRSKGR NRIHDWSYLI TRGLPSSIMK NLTRCWRSVV EEQMNKFLTA
SWKDDDFVPR YCERYYVLQK SSSELFGPRA AFLLAMRNGC ADAVLRLPFL RAAHVSEQFA
RHIDQRIQGS RMGGARGMEM LAQLQRCLES VLIFSPLEIA TTFEHYYQHY MADRLLSVGS
SWLEGAVLEQ IGPCFPSRLP QQMLQSLNVS EELQRQFHVY QLQQLDQELL KLEDTEKKIQ
VAHEDSGRED KSKKEEAIGE AAAVAMAEEE DQGKKEEGEE EGEGEDEEEE RYYKGTMPEV
CVLVVTPRFW PVASVCQMLN PATCLPAYLR GTINHYTNFY SKSQSRSSLE KEPQRRLQWT
WQGRAEVQFG GQILHVSTVQ MWLLLHLNNQ KEVSVESLQA ISELPPDVLH RAIGPLTSSR
GPLDLQEQKN VPGGVLKIRD DSEEPRPRRG NVWLIPPQTY LQAEAEEGRN MEKRRNLLNC
LVVRILKAHG DEGLHVDRLV YLVLEAWEKG PCPARGLVSS LGRGATCRSS DVLSCILHLL
VKGTLRRHDD RPQVLYYAVP VTVMEPHMES LNPGSAGPNP PLTFHTLQIR SRGVPYASCT
DNHTFSTFR
