ZCC17_HUMAN
ID ZCC17_HUMAN Reviewed; 241 AA.
AC Q9NP64; B4DY38; D3DPN4; Q6PKH4; Q9NYG4; Q9P0M8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger CCHC domain-containing protein 17;
DE AltName: Full=Nucleolar protein of 40 kDa {ECO:0000303|PubMed:12893261};
DE Short=pNO40 {ECO:0000303|PubMed:12893261};
DE AltName: Full=Pnn-interacting nucleolar protein;
DE AltName: Full=Putative S1 RNA-binding domain protein;
DE Short=PS1D protein;
GN Name=ZCCHC17; Synonyms=PS1D; ORFNames=HSPC243, HSPC251, LDC4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PNN.
RC TISSUE=Kidney;
RX PubMed=12893261; DOI=10.1016/s0006-291x(03)01208-7;
RA Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.;
RT "Molecular characterization of a novel nucleolar protein, pNO40.";
RL Biochem. Biophys. Res. Commun. 307:569-577(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, Retinoblastoma, Teratocarcinoma, and Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Muscle, and Uterus;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP STRUCTURE BY NMR OF 1-106.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the S1 RNA binding domain of human hypothetical
RT protein FLJ11067.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- SUBUNIT: Interacts with PNN. Associates with the 60S ribosomal subunit
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NP64; Q9BXS5: AP1M1; NbExp=7; IntAct=EBI-746345, EBI-541426;
CC Q9NP64; Q08426: EHHADH; NbExp=3; IntAct=EBI-746345, EBI-2339219;
CC Q9NP64; P22607: FGFR3; NbExp=3; IntAct=EBI-746345, EBI-348399;
CC Q9NP64; Q14957: GRIN2C; NbExp=3; IntAct=EBI-746345, EBI-8285963;
CC Q9NP64; P06396: GSN; NbExp=3; IntAct=EBI-746345, EBI-351506;
CC Q9NP64; Q6NYC1: JMJD6; NbExp=2; IntAct=EBI-746345, EBI-8464037;
CC Q9NP64; Q9BS40: LXN; NbExp=3; IntAct=EBI-746345, EBI-1044504;
CC Q9NP64; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746345, EBI-741158;
CC Q9NP64; P78317: RNF4; NbExp=3; IntAct=EBI-746345, EBI-2340927;
CC Q9NP64; O00560: SDCBP; NbExp=8; IntAct=EBI-746345, EBI-727004;
CC Q9NP64; Q9H190: SDCBP2; NbExp=8; IntAct=EBI-746345, EBI-742426;
CC Q9NP64; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-746345, EBI-12097232;
CC Q9NP64; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-746345, EBI-741480;
CC Q9NP64; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-746345, EBI-746345;
CC Q9NP64; P17020: ZNF16; NbExp=3; IntAct=EBI-746345, EBI-3921553;
CC Q9NP64; Q9Y649; NbExp=3; IntAct=EBI-746345, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12893261}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=hpNO40;
CC IsoId=Q9NP64-1; Sequence=Displayed;
CC Name=2; Synonyms=hpNO40s;
CC IsoId=Q9NP64-2; Sequence=VSP_015308;
CC Name=3;
CC IsoId=Q9NP64-3; Sequence=VSP_054531;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36171.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF247661; AAF72518.3; -; mRNA.
DR EMBL; AF151077; AAF36163.1; -; mRNA.
DR EMBL; AF151085; AAF36171.1; ALT_FRAME; mRNA.
DR EMBL; AK001929; BAA91984.1; -; mRNA.
DR EMBL; AK022506; BAB14066.1; -; mRNA.
DR EMBL; AK024049; BAB14799.1; -; mRNA.
DR EMBL; AK302248; BAG63600.1; -; mRNA.
DR EMBL; AL451070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07620.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07621.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07622.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07624.1; -; Genomic_DNA.
DR EMBL; BC000685; AAH00685.1; -; mRNA.
DR EMBL; BC007446; AAH07446.1; -; mRNA.
DR EMBL; BC050609; AAH50609.1; -; mRNA.
DR CCDS; CCDS341.1; -. [Q9NP64-1]
DR CCDS; CCDS60061.1; -. [Q9NP64-3]
DR RefSeq; NP_001269495.1; NM_001282566.1.
DR RefSeq; NP_001269496.1; NM_001282567.1.
DR RefSeq; NP_001269497.1; NM_001282568.1. [Q9NP64-1]
DR RefSeq; NP_001269498.1; NM_001282569.1. [Q9NP64-3]
DR RefSeq; NP_001269499.1; NM_001282570.1. [Q9NP64-2]
DR RefSeq; NP_001269500.1; NM_001282571.1.
DR RefSeq; NP_001269501.1; NM_001282572.1.
DR RefSeq; NP_001269502.1; NM_001282573.1.
DR RefSeq; NP_001269503.1; NM_001282574.1.
DR RefSeq; NP_057589.2; NM_016505.3. [Q9NP64-1]
DR RefSeq; XP_006710744.1; XM_006710681.3. [Q9NP64-3]
DR RefSeq; XP_011539869.1; XM_011541567.2.
DR PDB; 2CQO; NMR; -; A=1-106.
DR PDBsum; 2CQO; -.
DR AlphaFoldDB; Q9NP64; -.
DR SMR; Q9NP64; -.
DR BioGRID; 119598; 93.
DR IntAct; Q9NP64; 66.
DR MINT; Q9NP64; -.
DR STRING; 9606.ENSP00000480986; -.
DR iPTMnet; Q9NP64; -.
DR MetOSite; Q9NP64; -.
DR PhosphoSitePlus; Q9NP64; -.
DR SwissPalm; Q9NP64; -.
DR BioMuta; ZCCHC17; -.
DR DMDM; 73921227; -.
DR EPD; Q9NP64; -.
DR jPOST; Q9NP64; -.
DR MassIVE; Q9NP64; -.
DR MaxQB; Q9NP64; -.
DR PaxDb; Q9NP64; -.
DR PeptideAtlas; Q9NP64; -.
DR PRIDE; Q9NP64; -.
DR ProteomicsDB; 5494; -.
DR ProteomicsDB; 81894; -. [Q9NP64-1]
DR ProteomicsDB; 81895; -. [Q9NP64-2]
DR Antibodypedia; 31100; 196 antibodies from 23 providers.
DR DNASU; 51538; -.
DR Ensembl; ENST00000344147.10; ENSP00000343557.5; ENSG00000121766.16. [Q9NP64-1]
DR Ensembl; ENST00000373714.5; ENSP00000362819.1; ENSG00000121766.16. [Q9NP64-1]
DR Ensembl; ENST00000546109.5; ENSP00000444742.1; ENSG00000121766.16. [Q9NP64-3]
DR GeneID; 51538; -.
DR KEGG; hsa:51538; -.
DR MANE-Select; ENST00000344147.10; ENSP00000343557.5; NM_016505.4; NP_057589.2.
DR UCSC; uc001bsp.3; human. [Q9NP64-1]
DR CTD; 51538; -.
DR DisGeNET; 51538; -.
DR GeneCards; ZCCHC17; -.
DR HGNC; HGNC:30246; ZCCHC17.
DR HPA; ENSG00000121766; Low tissue specificity.
DR MIM; 619744; gene.
DR neXtProt; NX_Q9NP64; -.
DR OpenTargets; ENSG00000121766; -.
DR PharmGKB; PA142670539; -.
DR VEuPathDB; HostDB:ENSG00000121766; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00510000047363; -.
DR InParanoid; Q9NP64; -.
DR OrthoDB; 1462437at2759; -.
DR PhylomeDB; Q9NP64; -.
DR TreeFam; TF332136; -.
DR PathwayCommons; Q9NP64; -.
DR SignaLink; Q9NP64; -.
DR BioGRID-ORCS; 51538; 3 hits in 1076 CRISPR screens.
DR ChiTaRS; ZCCHC17; human.
DR EvolutionaryTrace; Q9NP64; -.
DR GeneWiki; ZCCHC17; -.
DR GenomeRNAi; 51538; -.
DR Pharos; Q9NP64; Tbio.
DR PRO; PR:Q9NP64; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NP64; protein.
DR Bgee; ENSG00000121766; Expressed in C1 segment of cervical spinal cord and 182 other tissues.
DR ExpressionAtlas; Q9NP64; baseline and differential.
DR Genevisible; Q9NP64; HS.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043489; P:RNA stabilization; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR037320; pNO40.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR15838:SF1; PTHR15838:SF1; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Zinc; Zinc-finger.
FT CHAIN 1..241
FT /note="Zinc finger CCHC domain-containing protein 17"
FT /id="PRO_0000096902"
FT DOMAIN 16..88
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT ZN_FING 131..148
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 161..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESX4"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12893261"
FT /id="VSP_015308"
FT VAR_SEQ 1..22
FT /note="MNSGRPETMENLPALYTIFQGE -> MKQLIEDTEKNKVY (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054531"
FT CONFLICT 217
FT /note="R -> G (in Ref. 2; AAF36171)"
FT /evidence="ECO:0000305"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:2CQO"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2CQO"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2CQO"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2CQO"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2CQO"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:2CQO"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2CQO"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2CQO"
SQ SEQUENCE 241 AA; 27570 MW; DA1B039DAC5F4A1D CRC64;
MNSGRPETME NLPALYTIFQ GEVAMVTDYG AFIKIPGCRK QGLVHRTHMS SCRVDKPSEI
VDVGDKVWVK LIGREMKNDR IKVSLSMKVV NQGTGKDLDP NNVIIEQEER RRRSFQDYTG
QKITLEAVLN TTCKKCGCKG HFAKDCFMQP GGTKYSLIPD EEEEKEEAKS AEFEKPDPTR
NPSRKRKKEK KKKKHRDRKS SDSDSSDSES DTGKRARHTS KDSKAAKKKK KKKKHKKKHK
E
