Full text data of ZZEF1
ZZEF1
(KIAA0399)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Zinc finger ZZ-type and EF-hand domain-containing protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc finger ZZ-type and EF-hand domain-containing protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43149
ID ZZEF1_HUMAN Reviewed; 2961 AA.
AC O43149; A7MBM5; Q6NXG0; Q6ZRA1; Q6ZSF4; Q9NVB9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 6.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Zinc finger ZZ-type and EF-hand domain-containing protein 1;
GN Name=ZZEF1; Synonyms=KIAA0399;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP PRO-1972; VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII.
RT 78 new cDNA clones from brain which code for large proteins in
RT vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1614-2961 (ISOFORM 2), AND VARIANT
RP ALA-30.
RC TISSUE=Teratocarcinoma, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP PRO-1972; VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15519529; DOI=10.1016/j.ejca.2004.08.005;
RA Cvekl A. Jr., Zavadil J., Birshtein B.K., Grotzer M.A., Cvekl A.;
RT "Analysis of transcripts from 17p13.3 in medulloblastoma suggests
RT ROX/MNT as a potential tumour suppressor gene.";
RL Eur. J. Cancer 40:2525-2532(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2667, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43149-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43149-2; Sequence=VSP_042268, VSP_042269, VSP_042270;
CC Note=Incomplete sequence. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=O43149-3; Sequence=VSP_036989, VSP_025870, VSP_025871;
CC Note=May be due to an intron retention. No experimental
CC confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in cerebellum.
CC -!- SIMILARITY: Contains 1 DOC domain.
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 2 ZZ-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23695.4; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA91834.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB007859; BAA23695.4; ALT_INIT; mRNA.
DR EMBL; AK001683; BAA91834.1; ALT_INIT; mRNA.
DR EMBL; AK127482; BAC86999.1; -; mRNA.
DR EMBL; AC067815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067099; AAH67099.1; -; mRNA.
DR EMBL; BC151836; AAI51837.1; -; mRNA.
DR PIR; T00048; T00048.
DR RefSeq; NP_055928.3; NM_015113.3.
DR UniGene; Hs.277624; -.
DR ProteinModelPortal; O43149; -.
DR SMR; O43149; 265-377.
DR IntAct; O43149; 5.
DR MINT; MINT-1191246; -.
DR PhosphoSite; O43149; -.
DR PaxDb; O43149; -.
DR PRIDE; O43149; -.
DR Ensembl; ENST00000381638; ENSP00000371051; ENSG00000074755.
DR GeneID; 23140; -.
DR KEGG; hsa:23140; -.
DR UCSC; uc002fxe.3; human.
DR CTD; 23140; -.
DR GeneCards; GC17M003854; -.
DR H-InvDB; HIX0017584; -.
DR HGNC; HGNC:29027; ZZEF1.
DR HPA; HPA031778; -.
DR HPA; HPA031790; -.
DR neXtProt; NX_O43149; -.
DR PharmGKB; PA134938508; -.
DR eggNOG; NOG254031; -.
DR HOGENOM; HOG000155817; -.
DR HOVERGEN; HBG108782; -.
DR InParanoid; O43149; -.
DR OMA; VHIPGAI; -.
DR OrthoDB; EOG76MK7D; -.
DR PhylomeDB; O43149; -.
DR ChiTaRS; ZZEF1; human.
DR GenomeRNAi; 23140; -.
DR NextBio; 44414; -.
DR PRO; PR:O43149; -.
DR ArrayExpress; O43149; -.
DR Bgee; O43149; -.
DR CleanEx; HS_ZZEF1; -.
DR Genevestigator; O43149; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 2.60.120.260; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR000433; Znf_ZZ.
DR Pfam; PF03256; APC10; 1.
DR Pfam; PF00569; ZZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Lipoprotein;
KW Metal-binding; Myristate; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 2961 Zinc finger ZZ-type and EF-hand domain-
FT containing protein 1.
FT /FTId=PRO_0000289000.
FT DOMAIN 111 146 EF-hand.
FT DOMAIN 226 405 DOC.
FT ZN_FING 1777 1825 ZZ-type 1.
FT ZN_FING 1826 1872 ZZ-type 2.
FT MOD_RES 1475 1475 Phosphoserine.
FT MOD_RES 1509 1509 Phosphoserine.
FT MOD_RES 1518 1518 Phosphoserine.
FT MOD_RES 1540 1540 Phosphoserine (By similarity).
FT MOD_RES 2667 2667 N6-acetyllysine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 1613 Missing (in isoform 2).
FT /FTId=VSP_042268.
FT VAR_SEQ 882 882 M -> MK (in isoform 3).
FT /FTId=VSP_036989.
FT VAR_SEQ 1079 1084 LDVETW -> VTRVST (in isoform 3).
FT /FTId=VSP_025870.
FT VAR_SEQ 1085 2961 Missing (in isoform 3).
FT /FTId=VSP_025871.
FT VAR_SEQ 2405 2424 ILSIMLYSSKKEINALAEHG -> VRDERDSCSSFLVQMCW
FT PRS (in isoform 2).
FT /FTId=VSP_042269.
FT VAR_SEQ 2425 2961 Missing (in isoform 2).
FT /FTId=VSP_042270.
FT VARIANT 30 30 V -> A (in dbSNP:rs1454121).
FT /FTId=VAR_032551.
FT VARIANT 1021 1021 I -> V (in dbSNP:rs16953687).
FT /FTId=VAR_032552.
FT VARIANT 1437 1437 S -> A (in dbSNP:rs4790555).
FT /FTId=VAR_032553.
FT VARIANT 1972 1972 L -> P (in dbSNP:rs781852).
FT /FTId=VAR_032554.
FT VARIANT 2014 2014 I -> V (in dbSNP:rs781831).
FT /FTId=VAR_032555.
FT VARIANT 2051 2051 P -> S (in dbSNP:rs1006954).
FT /FTId=VAR_032556.
FT VARIANT 2301 2301 Y -> H (in dbSNP:rs34357158).
FT /FTId=VAR_032557.
FT VARIANT 2303 2303 L -> P (in dbSNP:rs35638819).
FT /FTId=VAR_032558.
FT VARIANT 2369 2369 E -> Q (in dbSNP:rs711177).
FT /FTId=VAR_032559.
FT VARIANT 2421 2421 A -> T (in dbSNP:rs781861).
FT /FTId=VAR_032560.
FT CONFLICT 959 959 V -> A (in Ref. 1; BAA23695 and 5;
FT AAI51837).
FT CONFLICT 1929 1929 R -> H (in Ref. 3; BAA91834).
SQ SEQUENCE 2961 AA; 331075 MW; 0DB2EB72C16BC168 CRC64;
MGNAPSHSSE DEAAAAGGEG WGPHQDWAAV SGTTPGPGVA APALPPAAAL LEPARLREAA
AALLPTPPCE SLVSRHRGAL FRWLEERLGR GEESVTLEQF RELLEARGAG CSSEQFEEAF
AQFDAEGDGT VDAENMLEAL KNSSGANLQG ELSHIIRQLQ ACSLVPGFTD IFSESKEGLD
IHSSMILRFL HRNRLSSAVM PYPMLEHCNN MCTMRSSVLK ESLDQLVQKE KESPGDLTRS
PEMDKLKSVA KCYAYIETSS NSADIDKMTN GETSSYWQSD GSACSHWIRL KMKPDVVLRH
LSIAVAATDQ SYMPQQVTVA VGRNASDLQE VRDVHIPSNV TGYVTLLENA NVSQLYVQIN
IKRCLSDGCD TRIHGLRAVG FQRVKKSGVS VSDASAIWYW SLLTSLVTAS METNPAFVQT
VLHNTQKALR HMPPLSLSPG STDFSTFLSP NVLEEVDSFL IRITSCCSTP EVELTLLAFA
LARGSVAKVM SSLCTITDHL DTQYDASSLI LSMASVRQNL LLKYGKPLQL TLQACDVKGK
EDKSGPENLL VEPWTRDGFL TETGKTRAST IFSTGTESAF QVTQIRIMVR RGGIGAQCGL
VFAYNSSSDK FCAEEHFKRF EKYDKWKLQE LRQFVKSRIG CSSDDLGEDD PIGWFELEEE
WDEADVKLQQ CRVAKYLMVK FLCTRQESAE RLGVQGLTIS GYLRPARAEA EQSVTCAHCR
KDTEESVCGA TLLLRTLQFI QQLAHDLVQQ KESGLKYKSF LDFAGLDLQI FWNFYSKLKQ
NPREECVSAQ TLLLQLLQSC FSVLQGDVLA ASEEEKAPIQ SPKGVEAAKE LYTHLCDVVD
KVDGDSVPME ILKQEVRNTL LNGAAIFFPN RQTRRNHLFT MMNVTEQEHK QSLQLTFRSL
CTYFSDKDPG GLLLLPEKND LAKMNISEVL AVMDTLVSVA ARECELLMLS GAPGEVGSVL
FSLFWSVQGS LLSWCYLQLK STDSGAKDLA VDLIEKYVGQ FLASMRAILE SLFSQYSGKT
IVERLCNSVF SMAARQLVIF LLDFCTLDIP HCVLLREFSV LTELLKKLCS GPEGGLRKLD
VETWQQEQPV VLHTWTKESA HNYENNCHEV SVFVSPGATY FEVEFDDRCE TEKRYDYLEF
TDARGRKTRY DTKVGTDKWP KKVTFKAGPR LQFLFHSDSS HNEWGYKFTV TACGLPDVAV
SWGLDLQLLV SRLMGRLASQ CMALKSVRQL GSNMVVPQAK MALVLSSPLW KPVFRHQVCP
ELELEASWPT HPHRNSKEVK NIPDDPCRHF LLDFAQSEPA QNFCGPYSEL FKGFIQACRK
QAPKTDIVAG STIDQAVNAT FAALVYRTPD LYEKLQKYVN SGGKIALSEE FAQVYSLADG
IRIWMLEMKQ KSLMSLGNEA EEKHSSEATE VNPESLAKEC IEKSLLLLKF LPTGISSKES
CEKLETADET SHLQPLNKRQ RTSSVVEEHF QASVSPTEAA PPATGDQSPG LGTQPKLPSS
SGLPAADVSP ATAEEPLSPS TPTRRPPFTR GRLRLLSFRS MEEARLVPTV KEKYPVLKDV
MDFIKDQSLS HRSVVKVLSL RKAQAQSILE VLKITQHCAE SLGQPHCFHP PFILFLLELL
TCQKDFTNYF GHLEGCGADL HKEIRDTYYQ LVLFLVKAVK GFSSLNDRSL LPALSCVQTA
LLHLLDMGWE PNDLAFFVDI QLPDLLMKMS QENISVHDSV ISQWSEEDEL ADAKQNSEWM
DECQDGMFEA WYEKIAQEDP EKQRKMHMFI ARYCDLLNVD ISCDGCDEIA PWHRYRCLQC
SDMDLCKTCF LGGVKPEGHG DDHEMVNMEF TCDHCQGLII GRRMNCNVCD DFDLCYGCYA
AKKYSYGHLP THSITAHPMV TIRISDRQRL IQPYIHNYSW LLFAALALYS AHLASAEDVD
GEKLDPQTRS SATTLRSQCM QLVGDCLMKA HQGKGLKALA LLGVLPDGDS SLEDQALPVT
VPTGASEEQL EKKAVQGAEL SEAGNGKRAV HEEIRPVDFK QRNKADKGVS LSKDPSCQTQ
ISDSPADASP PTGLPDAEDS EVSSQKPIEE KAVTPSPEQV FAECSQKRIL GLLAAMLPPL
KSGPTVPLID LEHVLPLMFQ VVISNAGHLN ETYHLTLGLL GQLIIRLLPA EVDAAVIKVL
SAKHNLFAAG DSSIVPDGWK TTHLLFSLGA VCLDSRVGLD WACSMAEILR SLNSAPLWRD
VIATFTDHCI KQLPFQLKHT NIFTLLVLVG FPQVLCVGTR CVYMDNANEP HNVIILKHFT
EKNRAVIVDV KTRKRKTVKD YQLVQKGGGQ ECGDSRAQLS QYSQHFAFIA SHLLQSSMDS
HCPEAVEATW VLSLALKGLY KTLKAHGFEE IRATFLQTDL LKLLVKKCSK GTGFSKTWLL
RDLEILSIML YSSKKEINAL AEHGDLELDE RGDREEEVER PVSSPGDPEQ KKLDPLEGLD
EPTRICFLMA HDALNAPLHI LRAIYELQMK KTDYFFLEVQ KRFDGDELTT DERIRSLAQR
WQPSKSLRLE EQSAKAVDTD MIILPCLSRP ARCDQATAES NPVTQKLISS TESELQQSYA
KQRRSKSAAL LHKELNCKSK RAVRDYLFRV NEATAVLYAR HVLASLLAEW PSHVPVSEDI
LELSGPAHMT YILDMFMQLE EKHEWEKILQ KVLQGCREDM LGTMALAACQ FMEEPGMEVQ
VRESKHPYNN NTNFEDKVHI PGAIYLSIKF DSQCNTEEGC DELAMSSSSD FQQDRHSFSG
SQQKWKDFEL PGDTLYYRFT SDMSNTEWGY RFTVTAGHLG RFQTGFEILK QMLSEERVVP
HLPLAKIWEW LVGVACRQTG HQRLKAIHLL LRIVRCCGHS DLCDLALLKP LWQLFTHMEY
GLFEDVTQPG ILLPLHRALT ELFFVTENRA QELGVLQDYL LALTTDDHLL RCAAQALQNI
AAISLAINYP NKATRLWNVE C
//
ID ZZEF1_HUMAN Reviewed; 2961 AA.
AC O43149; A7MBM5; Q6NXG0; Q6ZRA1; Q6ZSF4; Q9NVB9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 6.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Zinc finger ZZ-type and EF-hand domain-containing protein 1;
GN Name=ZZEF1; Synonyms=KIAA0399;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP PRO-1972; VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII.
RT 78 new cDNA clones from brain which code for large proteins in
RT vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1614-2961 (ISOFORM 2), AND VARIANT
RP ALA-30.
RC TISSUE=Teratocarcinoma, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP PRO-1972; VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15519529; DOI=10.1016/j.ejca.2004.08.005;
RA Cvekl A. Jr., Zavadil J., Birshtein B.K., Grotzer M.A., Cvekl A.;
RT "Analysis of transcripts from 17p13.3 in medulloblastoma suggests
RT ROX/MNT as a potential tumour suppressor gene.";
RL Eur. J. Cancer 40:2525-2532(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2667, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43149-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43149-2; Sequence=VSP_042268, VSP_042269, VSP_042270;
CC Note=Incomplete sequence. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=O43149-3; Sequence=VSP_036989, VSP_025870, VSP_025871;
CC Note=May be due to an intron retention. No experimental
CC confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in cerebellum.
CC -!- SIMILARITY: Contains 1 DOC domain.
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 2 ZZ-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23695.4; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA91834.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB007859; BAA23695.4; ALT_INIT; mRNA.
DR EMBL; AK001683; BAA91834.1; ALT_INIT; mRNA.
DR EMBL; AK127482; BAC86999.1; -; mRNA.
DR EMBL; AC067815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067099; AAH67099.1; -; mRNA.
DR EMBL; BC151836; AAI51837.1; -; mRNA.
DR PIR; T00048; T00048.
DR RefSeq; NP_055928.3; NM_015113.3.
DR UniGene; Hs.277624; -.
DR ProteinModelPortal; O43149; -.
DR SMR; O43149; 265-377.
DR IntAct; O43149; 5.
DR MINT; MINT-1191246; -.
DR PhosphoSite; O43149; -.
DR PaxDb; O43149; -.
DR PRIDE; O43149; -.
DR Ensembl; ENST00000381638; ENSP00000371051; ENSG00000074755.
DR GeneID; 23140; -.
DR KEGG; hsa:23140; -.
DR UCSC; uc002fxe.3; human.
DR CTD; 23140; -.
DR GeneCards; GC17M003854; -.
DR H-InvDB; HIX0017584; -.
DR HGNC; HGNC:29027; ZZEF1.
DR HPA; HPA031778; -.
DR HPA; HPA031790; -.
DR neXtProt; NX_O43149; -.
DR PharmGKB; PA134938508; -.
DR eggNOG; NOG254031; -.
DR HOGENOM; HOG000155817; -.
DR HOVERGEN; HBG108782; -.
DR InParanoid; O43149; -.
DR OMA; VHIPGAI; -.
DR OrthoDB; EOG76MK7D; -.
DR PhylomeDB; O43149; -.
DR ChiTaRS; ZZEF1; human.
DR GenomeRNAi; 23140; -.
DR NextBio; 44414; -.
DR PRO; PR:O43149; -.
DR ArrayExpress; O43149; -.
DR Bgee; O43149; -.
DR CleanEx; HS_ZZEF1; -.
DR Genevestigator; O43149; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 2.60.120.260; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR000433; Znf_ZZ.
DR Pfam; PF03256; APC10; 1.
DR Pfam; PF00569; ZZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Lipoprotein;
KW Metal-binding; Myristate; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 2961 Zinc finger ZZ-type and EF-hand domain-
FT containing protein 1.
FT /FTId=PRO_0000289000.
FT DOMAIN 111 146 EF-hand.
FT DOMAIN 226 405 DOC.
FT ZN_FING 1777 1825 ZZ-type 1.
FT ZN_FING 1826 1872 ZZ-type 2.
FT MOD_RES 1475 1475 Phosphoserine.
FT MOD_RES 1509 1509 Phosphoserine.
FT MOD_RES 1518 1518 Phosphoserine.
FT MOD_RES 1540 1540 Phosphoserine (By similarity).
FT MOD_RES 2667 2667 N6-acetyllysine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 1613 Missing (in isoform 2).
FT /FTId=VSP_042268.
FT VAR_SEQ 882 882 M -> MK (in isoform 3).
FT /FTId=VSP_036989.
FT VAR_SEQ 1079 1084 LDVETW -> VTRVST (in isoform 3).
FT /FTId=VSP_025870.
FT VAR_SEQ 1085 2961 Missing (in isoform 3).
FT /FTId=VSP_025871.
FT VAR_SEQ 2405 2424 ILSIMLYSSKKEINALAEHG -> VRDERDSCSSFLVQMCW
FT PRS (in isoform 2).
FT /FTId=VSP_042269.
FT VAR_SEQ 2425 2961 Missing (in isoform 2).
FT /FTId=VSP_042270.
FT VARIANT 30 30 V -> A (in dbSNP:rs1454121).
FT /FTId=VAR_032551.
FT VARIANT 1021 1021 I -> V (in dbSNP:rs16953687).
FT /FTId=VAR_032552.
FT VARIANT 1437 1437 S -> A (in dbSNP:rs4790555).
FT /FTId=VAR_032553.
FT VARIANT 1972 1972 L -> P (in dbSNP:rs781852).
FT /FTId=VAR_032554.
FT VARIANT 2014 2014 I -> V (in dbSNP:rs781831).
FT /FTId=VAR_032555.
FT VARIANT 2051 2051 P -> S (in dbSNP:rs1006954).
FT /FTId=VAR_032556.
FT VARIANT 2301 2301 Y -> H (in dbSNP:rs34357158).
FT /FTId=VAR_032557.
FT VARIANT 2303 2303 L -> P (in dbSNP:rs35638819).
FT /FTId=VAR_032558.
FT VARIANT 2369 2369 E -> Q (in dbSNP:rs711177).
FT /FTId=VAR_032559.
FT VARIANT 2421 2421 A -> T (in dbSNP:rs781861).
FT /FTId=VAR_032560.
FT CONFLICT 959 959 V -> A (in Ref. 1; BAA23695 and 5;
FT AAI51837).
FT CONFLICT 1929 1929 R -> H (in Ref. 3; BAA91834).
SQ SEQUENCE 2961 AA; 331075 MW; 0DB2EB72C16BC168 CRC64;
MGNAPSHSSE DEAAAAGGEG WGPHQDWAAV SGTTPGPGVA APALPPAAAL LEPARLREAA
AALLPTPPCE SLVSRHRGAL FRWLEERLGR GEESVTLEQF RELLEARGAG CSSEQFEEAF
AQFDAEGDGT VDAENMLEAL KNSSGANLQG ELSHIIRQLQ ACSLVPGFTD IFSESKEGLD
IHSSMILRFL HRNRLSSAVM PYPMLEHCNN MCTMRSSVLK ESLDQLVQKE KESPGDLTRS
PEMDKLKSVA KCYAYIETSS NSADIDKMTN GETSSYWQSD GSACSHWIRL KMKPDVVLRH
LSIAVAATDQ SYMPQQVTVA VGRNASDLQE VRDVHIPSNV TGYVTLLENA NVSQLYVQIN
IKRCLSDGCD TRIHGLRAVG FQRVKKSGVS VSDASAIWYW SLLTSLVTAS METNPAFVQT
VLHNTQKALR HMPPLSLSPG STDFSTFLSP NVLEEVDSFL IRITSCCSTP EVELTLLAFA
LARGSVAKVM SSLCTITDHL DTQYDASSLI LSMASVRQNL LLKYGKPLQL TLQACDVKGK
EDKSGPENLL VEPWTRDGFL TETGKTRAST IFSTGTESAF QVTQIRIMVR RGGIGAQCGL
VFAYNSSSDK FCAEEHFKRF EKYDKWKLQE LRQFVKSRIG CSSDDLGEDD PIGWFELEEE
WDEADVKLQQ CRVAKYLMVK FLCTRQESAE RLGVQGLTIS GYLRPARAEA EQSVTCAHCR
KDTEESVCGA TLLLRTLQFI QQLAHDLVQQ KESGLKYKSF LDFAGLDLQI FWNFYSKLKQ
NPREECVSAQ TLLLQLLQSC FSVLQGDVLA ASEEEKAPIQ SPKGVEAAKE LYTHLCDVVD
KVDGDSVPME ILKQEVRNTL LNGAAIFFPN RQTRRNHLFT MMNVTEQEHK QSLQLTFRSL
CTYFSDKDPG GLLLLPEKND LAKMNISEVL AVMDTLVSVA ARECELLMLS GAPGEVGSVL
FSLFWSVQGS LLSWCYLQLK STDSGAKDLA VDLIEKYVGQ FLASMRAILE SLFSQYSGKT
IVERLCNSVF SMAARQLVIF LLDFCTLDIP HCVLLREFSV LTELLKKLCS GPEGGLRKLD
VETWQQEQPV VLHTWTKESA HNYENNCHEV SVFVSPGATY FEVEFDDRCE TEKRYDYLEF
TDARGRKTRY DTKVGTDKWP KKVTFKAGPR LQFLFHSDSS HNEWGYKFTV TACGLPDVAV
SWGLDLQLLV SRLMGRLASQ CMALKSVRQL GSNMVVPQAK MALVLSSPLW KPVFRHQVCP
ELELEASWPT HPHRNSKEVK NIPDDPCRHF LLDFAQSEPA QNFCGPYSEL FKGFIQACRK
QAPKTDIVAG STIDQAVNAT FAALVYRTPD LYEKLQKYVN SGGKIALSEE FAQVYSLADG
IRIWMLEMKQ KSLMSLGNEA EEKHSSEATE VNPESLAKEC IEKSLLLLKF LPTGISSKES
CEKLETADET SHLQPLNKRQ RTSSVVEEHF QASVSPTEAA PPATGDQSPG LGTQPKLPSS
SGLPAADVSP ATAEEPLSPS TPTRRPPFTR GRLRLLSFRS MEEARLVPTV KEKYPVLKDV
MDFIKDQSLS HRSVVKVLSL RKAQAQSILE VLKITQHCAE SLGQPHCFHP PFILFLLELL
TCQKDFTNYF GHLEGCGADL HKEIRDTYYQ LVLFLVKAVK GFSSLNDRSL LPALSCVQTA
LLHLLDMGWE PNDLAFFVDI QLPDLLMKMS QENISVHDSV ISQWSEEDEL ADAKQNSEWM
DECQDGMFEA WYEKIAQEDP EKQRKMHMFI ARYCDLLNVD ISCDGCDEIA PWHRYRCLQC
SDMDLCKTCF LGGVKPEGHG DDHEMVNMEF TCDHCQGLII GRRMNCNVCD DFDLCYGCYA
AKKYSYGHLP THSITAHPMV TIRISDRQRL IQPYIHNYSW LLFAALALYS AHLASAEDVD
GEKLDPQTRS SATTLRSQCM QLVGDCLMKA HQGKGLKALA LLGVLPDGDS SLEDQALPVT
VPTGASEEQL EKKAVQGAEL SEAGNGKRAV HEEIRPVDFK QRNKADKGVS LSKDPSCQTQ
ISDSPADASP PTGLPDAEDS EVSSQKPIEE KAVTPSPEQV FAECSQKRIL GLLAAMLPPL
KSGPTVPLID LEHVLPLMFQ VVISNAGHLN ETYHLTLGLL GQLIIRLLPA EVDAAVIKVL
SAKHNLFAAG DSSIVPDGWK TTHLLFSLGA VCLDSRVGLD WACSMAEILR SLNSAPLWRD
VIATFTDHCI KQLPFQLKHT NIFTLLVLVG FPQVLCVGTR CVYMDNANEP HNVIILKHFT
EKNRAVIVDV KTRKRKTVKD YQLVQKGGGQ ECGDSRAQLS QYSQHFAFIA SHLLQSSMDS
HCPEAVEATW VLSLALKGLY KTLKAHGFEE IRATFLQTDL LKLLVKKCSK GTGFSKTWLL
RDLEILSIML YSSKKEINAL AEHGDLELDE RGDREEEVER PVSSPGDPEQ KKLDPLEGLD
EPTRICFLMA HDALNAPLHI LRAIYELQMK KTDYFFLEVQ KRFDGDELTT DERIRSLAQR
WQPSKSLRLE EQSAKAVDTD MIILPCLSRP ARCDQATAES NPVTQKLISS TESELQQSYA
KQRRSKSAAL LHKELNCKSK RAVRDYLFRV NEATAVLYAR HVLASLLAEW PSHVPVSEDI
LELSGPAHMT YILDMFMQLE EKHEWEKILQ KVLQGCREDM LGTMALAACQ FMEEPGMEVQ
VRESKHPYNN NTNFEDKVHI PGAIYLSIKF DSQCNTEEGC DELAMSSSSD FQQDRHSFSG
SQQKWKDFEL PGDTLYYRFT SDMSNTEWGY RFTVTAGHLG RFQTGFEILK QMLSEERVVP
HLPLAKIWEW LVGVACRQTG HQRLKAIHLL LRIVRCCGHS DLCDLALLKP LWQLFTHMEY
GLFEDVTQPG ILLPLHRALT ELFFVTENRA QELGVLQDYL LALTTDDHLL RCAAQALQNI
AAISLAINYP NKATRLWNVE C
//