ZN618_HUMAN
ID ZN618_HUMAN Reviewed; 954 AA.
AC Q5T7W0; B9EG82; Q4G0X6; Q5T7W1; Q6ZT53; Q7Z6B9; Q8TF49; Q96E49;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein 618;
GN Name=ZNF618; Synonyms=KIAA1952;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Eye, Kidney, and Testis;
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 IDENTIFICATION BY 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63 AND LYS-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP FUNCTION, INTERACTION WITH UHRF2, AND SUBCELLULAR LOCATION.
RX PubMed=27129234; DOI=10.1074/jbc.m116.717314;
RA Liu Y., Zhang B., Kuang H., Korakavi G., Lu L.Y., Yu X.;
RT "Zinc Finger Protein 618 Regulates the Function of UHRF2 (Ubiquitin-like
RT with PHD and Ring Finger Domains 2) as a Specific 5-Hydroxymethylcytosine
RT Reader.";
RL J. Biol. Chem. 291:13679-13688(2016).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-81; LYS-239 AND LYS-437,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Regulates UHRF2 function as a specific 5-
CC hydroxymethylcytosine (5hmC) reader by regulating its chromatin
CC localization. {ECO:0000269|PubMed:27129234}.
CC -!- SUBUNIT: Interacts with UHRF2. {ECO:0000269|PubMed:27129234}.
CC -!- INTERACTION:
CC Q5T7W0; P48730: CSNK1D; NbExp=3; IntAct=EBI-6255994, EBI-751621;
CC Q5T7W0; P49674: CSNK1E; NbExp=5; IntAct=EBI-6255994, EBI-749343;
CC Q5T7W0; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-6255994, EBI-12082590;
CC Q5T7W0; Q9UN86-2: G3BP2; NbExp=3; IntAct=EBI-6255994, EBI-11035716;
CC Q5T7W0; O15344: MID1; NbExp=3; IntAct=EBI-6255994, EBI-2340316;
CC Q5T7W0; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-6255994, EBI-741158;
CC Q5T7W0; Q9NVG8: TBC1D13; NbExp=3; IntAct=EBI-6255994, EBI-12264956;
CC Q5T7W0; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-6255994, EBI-10180829;
CC Q5T7W0; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-6255994, EBI-607755;
CC Q5T7W0; Q5T7W0: ZNF618; NbExp=7; IntAct=EBI-6255994, EBI-6255994;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27129234}. Chromosome
CC {ECO:0000269|PubMed:27129234}. Note=Localizes at genomic loci that are
CC enriched for 5-hydroxymethylcytosine (5hmC).
CC {ECO:0000269|PubMed:27129234}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5T7W0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T7W0-2; Sequence=VSP_025179, VSP_025180, VSP_025181;
CC Name=3;
CC IsoId=Q5T7W0-3; Sequence=VSP_025179, VSP_025182, VSP_025183;
CC Name=4;
CC IsoId=Q5T7W0-4; Sequence=VSP_025179, VSP_055968;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36039.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB85538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB075832; BAB85538.1; ALT_INIT; mRNA.
DR EMBL; AK126896; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL137850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036039; AAH36039.1; ALT_SEQ; mRNA.
DR EMBL; BC053892; AAH53892.1; ALT_INIT; mRNA.
DR EMBL; BC012922; AAH12922.1; -; mRNA.
DR EMBL; BC136287; AAI36288.1; -; mRNA.
DR CCDS; CCDS48008.1; -. [Q5T7W0-2]
DR CCDS; CCDS83402.1; -. [Q5T7W0-1]
DR CCDS; CCDS83403.1; -. [Q5T7W0-4]
DR RefSeq; NP_001304969.1; NM_001318040.1. [Q5T7W0-4]
DR RefSeq; NP_001304970.1; NM_001318041.1.
DR RefSeq; NP_001304971.1; NM_001318042.1. [Q5T7W0-1]
DR RefSeq; NP_588615.2; NM_133374.2. [Q5T7W0-2]
DR AlphaFoldDB; Q5T7W0; -.
DR SMR; Q5T7W0; -.
DR BioGRID; 125407; 30.
DR IntAct; Q5T7W0; 13.
DR iPTMnet; Q5T7W0; -.
DR PhosphoSitePlus; Q5T7W0; -.
DR BioMuta; ZNF618; -.
DR DMDM; 74762243; -.
DR EPD; Q5T7W0; -.
DR jPOST; Q5T7W0; -.
DR MassIVE; Q5T7W0; -.
DR MaxQB; Q5T7W0; -.
DR PeptideAtlas; Q5T7W0; -.
DR PRIDE; Q5T7W0; -.
DR ProteomicsDB; 64691; -. [Q5T7W0-1]
DR ProteomicsDB; 64692; -. [Q5T7W0-2]
DR ProteomicsDB; 64693; -. [Q5T7W0-3]
DR Antibodypedia; 29860; 36 antibodies from 14 providers.
DR DNASU; 114991; -.
DR Ensembl; ENST00000288466.11; ENSP00000288466.7; ENSG00000157657.15. [Q5T7W0-2]
DR Ensembl; ENST00000374126.10; ENSP00000363241.5; ENSG00000157657.15. [Q5T7W0-1]
DR Ensembl; ENST00000615615.4; ENSP00000483198.1; ENSG00000157657.15. [Q5T7W0-4]
DR GeneID; 114991; -.
DR KEGG; hsa:114991; -.
DR MANE-Select; ENST00000374126.10; ENSP00000363241.5; NM_001318042.2; NP_001304971.1.
DR UCSC; uc004bic.4; human. [Q5T7W0-1]
DR CTD; 114991; -.
DR DisGeNET; 114991; -.
DR GeneCards; ZNF618; -.
DR HGNC; HGNC:29416; ZNF618.
DR HPA; ENSG00000157657; Low tissue specificity.
DR neXtProt; NX_Q5T7W0; -.
DR OpenTargets; ENSG00000157657; -.
DR PharmGKB; PA31532; -.
DR VEuPathDB; HostDB:ENSG00000157657; -.
DR GeneTree; ENSGT00940000153306; -.
DR HOGENOM; CLU_315147_0_0_1; -.
DR InParanoid; Q5T7W0; -.
DR OMA; QYWGSAV; -.
DR OrthoDB; 118368at2759; -.
DR PhylomeDB; Q5T7W0; -.
DR TreeFam; TF331270; -.
DR PathwayCommons; Q5T7W0; -.
DR SignaLink; Q5T7W0; -.
DR BioGRID-ORCS; 114991; 5 hits in 1084 CRISPR screens.
DR ChiTaRS; ZNF618; human.
DR GenomeRNAi; 114991; -.
DR Pharos; Q5T7W0; Tdark.
DR PRO; PR:Q5T7W0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T7W0; protein.
DR Bgee; ENSG00000157657; Expressed in secondary oocyte and 165 other tissues.
DR ExpressionAtlas; Q5T7W0; baseline and differential.
DR Genevisible; Q5T7W0; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IDA:ARUK-UCL.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..954
FT /note="Zinc finger protein 618"
FT /id="PRO_0000286811"
FT ZN_FING 147..169
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 113..144
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025179"
FT VAR_SEQ 252
FT /note="K -> MNNITSDIFKKKEVRQCQKRE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025180"
FT VAR_SEQ 282..363
FT /note="STAPGWEPPDDPDTGSECSHPEVSPSPRFVAAKTQTNQSGKKAPASVVRCAT
FT LLHRTPPATQTQTFRTPNSGSPASKATAAE -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025181"
FT VAR_SEQ 283..313
FT /note="TAPGWEPPDDPDTGSECSHPEVSPSPRFVAA -> EYLLPVGMGVGGPGTGW
FT ASRWPGLWNLARKW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025182"
FT VAR_SEQ 314..954
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025183"
FT VAR_SEQ 361
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055968"
FT CONFLICT 211
FT /note="A -> T (in Ref. 4; AAI36288)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="I -> V (in Ref. 4; AAH36039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 954 AA; 104956 MW; A50304AA0D61B92E CRC64;
MNQPGGAAAP QADGASAAGR KSTASRERLK RSQKSTKVEG PEPVPAEASL SAEQGTMTEV
KVKTELPDDY IQEVIWQGEA KEEKKAVSKD GTSDVPAEIC VVIGGVRNQQ TLDGKAPEGS
PHGGSVRSRY SGTWIFDQAL RYASGSYECG ICGKKYKYYN CFQTHVRAHR DTEATSGEGA
SQSNNFRYTC DICGKKYKYY SCFQEHRDLH AVDVFSVEGA PENRADPFDQ GVVATDEVKE
EPPEPFQKIG PKTGNYTCEF CGKQYKYYTP YQEHVALHAP ISTAPGWEPP DDPDTGSECS
HPEVSPSPRF VAAKTQTNQS GKKAPASVVR CATLLHRTPP ATQTQTFRTP NSGSPASKAT
AAESAFSRRV EGKAQNHFEE TNSSSQNSSE PYTCGACGIQ FQFYNNLLEH MQSHAADNEN
NIASNQSRSP PAVVEEKWKP QAQRNSANNT TTSGLTPNSM IPEKERQNIA ERLLRVMCAD
LGALSVVSGK EFLKLAQTLV DSGARYGAFS VTEILGNFNT LALKHLPRMY NQVKVKVTCA
LGSNACLGIG VTCHSQSVGP DSCYILTAYQ AEGNHIKSYV LGVKGADIRD SGDLVHHWVQ
NVLSEFVMSE IRTVYVTDCR VSTSAFSKAG MCLRCSACAL NSVVQSVLSK RTLQARSMHE
VIELLNVCED LAGSTGLAKE TFGSLEETSP PPCWNSVTDS LLLVHERYEQ ICEFYSRAKK
MNLIQSLNKH LLSNLAAILT PVKQAVIELS NESQPTLQLV LPTYVRLEKL FTAKANDAGT
VSKLCHLFLE ALKENFKVHP AHKVAMILDP QQKLRPVPPY QHEEIIGKVC ELINEVKESW
AEEADFEPAA KKPRSAAVEN PAAQEDDRLG KNEVYDYLQE PLFQATPDLF QYWSCVTQKH
TKLAKLAFWL LAVPAVGARS GCVNMCEQAL LIKRRRLLSP EDMNKLMFLK SNML
