ZXDC_HUMAN
ID ZXDC_HUMAN Reviewed; 858 AA.
AC Q2QGD7; C5J0H9; Q6DKI8; Q7L3L1; Q8NAU2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein ZXDC;
DE AltName: Full=ZXD-like zinc finger protein;
GN Name=ZXDC; Synonyms=ZXDL;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH CIITA,
RP AND TISSUE SPECIFICITY.
RX PubMed=16600381; DOI=10.1016/j.molimm.2006.02.029;
RA Al-Kandari W., Jambunathan S., Navalgund V., Koneni R., Freer M.,
RA Parimi N., Mudhasani R., Fontes J.D.;
RT "ZXDC, a novel zinc finger protein that binds CIITA and activates MHC gene
RT transcription.";
RL Mol. Immunol. 44:311-321(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT LEU-562.
RX PubMed=19777325; DOI=10.1007/s11010-009-0280-5;
RA Aleksandrova A., Galkin O., Koneni R., Fontes J.D.;
RT "An N- and C-terminal truncated isoform of zinc finger X-linked duplicated
RT C protein represses MHC class II transcription.";
RL Mol. Cell. Biochem. 337:1-7(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tang W.W., Tang Z.H., Yu L.;
RT "Cloning and characterization of the ZXDL gene which encodes a putative
RT zinc finger protein.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-858 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-858 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-710 (ISOFORM 2).
RC TISSUE=Placenta, Skin, 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 [7]
RP SUMOYLATION AT LYS-660, AND FUNCTION.
RX PubMed=17696781; DOI=10.1515/bc.2007.106;
RA Jambunathan S., Fontes J.D.;
RT "Sumoylation of the zinc finger protein ZXDC enhances the function of its
RT transcriptional activation domain.";
RL Biol. Chem. 388:965-972(2007).
RN [8]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH ZXDA AND CIITA.
RX PubMed=17493635; DOI=10.1016/j.jmb.2007.04.033;
RA Al-Kandari W., Koneni R., Navalgund V., Aleksandrova A., Jambunathan S.,
RA Fontes J.D.;
RT "The zinc finger proteins ZXDA and ZXDC form a complex that binds CIITA and
RT regulates MHC II gene transcription.";
RL J. Mol. Biol. 369:1175-1187(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND THR-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Cooperates with CIITA to promote transcription of MHC class I
CC and MHC class II genes. {ECO:0000269|PubMed:16600381,
CC ECO:0000269|PubMed:17493635, ECO:0000269|PubMed:17696781}.
CC -!- SUBUNIT: Self-associates. Interacts with ZXDA and CIITA.
CC {ECO:0000269|PubMed:16600381, ECO:0000269|PubMed:17493635}.
CC -!- INTERACTION:
CC Q2QGD7; P54253: ATXN1; NbExp=7; IntAct=EBI-1538838, EBI-930964;
CC Q2QGD7; P46379-2: BAG6; NbExp=3; IntAct=EBI-1538838, EBI-10988864;
CC Q2QGD7; Q8N4T8: CBR4; NbExp=3; IntAct=EBI-1538838, EBI-10897344;
CC Q2QGD7; P33076: CIITA; NbExp=6; IntAct=EBI-1538838, EBI-1538819;
CC Q2QGD7; O14645: DNALI1; NbExp=3; IntAct=EBI-1538838, EBI-395638;
CC Q2QGD7; P04792: HSPB1; NbExp=3; IntAct=EBI-1538838, EBI-352682;
CC Q2QGD7; P42858: HTT; NbExp=3; IntAct=EBI-1538838, EBI-466029;
CC Q2QGD7; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1538838, EBI-10975473;
CC Q2QGD7; O14901: KLF11; NbExp=3; IntAct=EBI-1538838, EBI-948266;
CC Q2QGD7; Q9NQ76: MEPE; NbExp=3; IntAct=EBI-1538838, EBI-1753293;
CC Q2QGD7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1538838, EBI-25882629;
CC Q2QGD7; Q7Z3K3: POGZ; NbExp=4; IntAct=EBI-1538838, EBI-1389308;
CC Q2QGD7; P60891: PRPS1; NbExp=3; IntAct=EBI-1538838, EBI-749195;
CC Q2QGD7; P49810: PSEN2; NbExp=3; IntAct=EBI-1538838, EBI-2010251;
CC Q2QGD7; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1538838, EBI-396669;
CC Q2QGD7; P00441: SOD1; NbExp=3; IntAct=EBI-1538838, EBI-990792;
CC Q2QGD7; P51687: SUOX; NbExp=3; IntAct=EBI-1538838, EBI-3921347;
CC Q2QGD7; P02766: TTR; NbExp=3; IntAct=EBI-1538838, EBI-711909;
CC Q2QGD7; P61964: WDR5; NbExp=5; IntAct=EBI-1538838, EBI-540834;
CC Q2QGD7; O76024: WFS1; NbExp=3; IntAct=EBI-1538838, EBI-720609;
CC Q2QGD7; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1538838, EBI-746595;
CC Q2QGD7; P98168: ZXDA; NbExp=5; IntAct=EBI-1538838, EBI-1538980;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2QGD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2QGD7-2; Sequence=VSP_026437, VSP_026438;
CC Name=3; Synonyms=ZXDC2;
CC IsoId=Q2QGD7-3; Sequence=VSP_047464, VSP_026437, VSP_026438;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, kidney, liver
CC and testis, at moderate levels in brain and stomach, and at low levels
CC in lung, muscle, placenta, small intestine and spleen.
CC {ECO:0000269|PubMed:16600381}.
CC -!- PTM: Sumoylated at Lys-660 with SUMO1, SUMO2 and SUMO3; sumoylation
CC enhances the activity of the transcriptional activation domain.
CC {ECO:0000269|PubMed:17696781}.
CC -!- MISCELLANEOUS: [Isoform 3]: Doesn't interact with CIITA. Represses MHC
CC class II transcription possibly via dominant-negative association with
CC isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZXD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY936556; AAX23974.1; -; mRNA.
DR EMBL; FJ980275; ACR56328.1; -; mRNA.
DR EMBL; DQ079590; AAZ30918.1; -; mRNA.
DR EMBL; AC024558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK092101; BAC03805.1; ALT_INIT; mRNA.
DR EMBL; BC002940; AAH02940.2; -; mRNA.
DR EMBL; BC012729; AAH12729.2; -; mRNA.
DR EMBL; BC073859; AAH73859.1; -; mRNA.
DR CCDS; CCDS43145.1; -. [Q2QGD7-1]
DR CCDS; CCDS43146.1; -. [Q2QGD7-2]
DR RefSeq; NP_001035743.1; NM_001040653.3. [Q2QGD7-2]
DR RefSeq; NP_079388.3; NM_025112.4. [Q2QGD7-1]
DR AlphaFoldDB; Q2QGD7; -.
DR SMR; Q2QGD7; -.
DR BioGRID; 122653; 24.
DR IntAct; Q2QGD7; 32.
DR MINT; Q2QGD7; -.
DR STRING; 9606.ENSP00000374359; -.
DR iPTMnet; Q2QGD7; -.
DR PhosphoSitePlus; Q2QGD7; -.
DR BioMuta; ZXDC; -.
DR DMDM; 296453026; -.
DR EPD; Q2QGD7; -.
DR jPOST; Q2QGD7; -.
DR MassIVE; Q2QGD7; -.
DR MaxQB; Q2QGD7; -.
DR PaxDb; Q2QGD7; -.
DR PeptideAtlas; Q2QGD7; -.
DR PRIDE; Q2QGD7; -.
DR ProteomicsDB; 61437; -. [Q2QGD7-1]
DR ProteomicsDB; 61438; -. [Q2QGD7-2]
DR Antibodypedia; 33073; 111 antibodies from 20 providers.
DR DNASU; 79364; -.
DR Ensembl; ENST00000336332.5; ENSP00000337694.5; ENSG00000070476.15. [Q2QGD7-2]
DR Ensembl; ENST00000389709.8; ENSP00000374359.3; ENSG00000070476.15. [Q2QGD7-1]
DR GeneID; 79364; -.
DR KEGG; hsa:79364; -.
DR MANE-Select; ENST00000389709.8; ENSP00000374359.3; NM_025112.5; NP_079388.3.
DR UCSC; uc003eiv.3; human. [Q2QGD7-1]
DR CTD; 79364; -.
DR DisGeNET; 79364; -.
DR GeneCards; ZXDC; -.
DR HGNC; HGNC:28160; ZXDC.
DR HPA; ENSG00000070476; Tissue enhanced (bone).
DR MIM; 615746; gene.
DR neXtProt; NX_Q2QGD7; -.
DR OpenTargets; ENSG00000070476; -.
DR PharmGKB; PA142670466; -.
DR VEuPathDB; HostDB:ENSG00000070476; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162216; -.
DR HOGENOM; CLU_007312_0_0_1; -.
DR InParanoid; Q2QGD7; -.
DR OMA; QCIQIPV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q2QGD7; -.
DR TreeFam; TF330996; -.
DR PathwayCommons; Q2QGD7; -.
DR SignaLink; Q2QGD7; -.
DR BioGRID-ORCS; 79364; 18 hits in 1102 CRISPR screens.
DR ChiTaRS; ZXDC; human.
DR GenomeRNAi; 79364; -.
DR Pharos; Q2QGD7; Tbio.
DR PRO; PR:Q2QGD7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q2QGD7; protein.
DR Bgee; ENSG00000070476; Expressed in gastrocnemius and 187 other tissues.
DR ExpressionAtlas; Q2QGD7; baseline and differential.
DR Genevisible; Q2QGD7; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..858
FT /note="Zinc finger protein ZXDC"
FT /id="PRO_0000292803"
FT ZN_FING 175..199
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 208..232
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 238..262
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..321
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..352
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..382
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..412
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..442
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..476
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..688
FT /note="Required for transcriptional activation"
FT REGION 660..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..858
FT /note="Interaction with CIITA"
FT REGION 837..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17696781"
FT VAR_SEQ 1..258
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19777325"
FT /id="VSP_047464"
FT VAR_SEQ 710
FT /note="E -> V (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19777325"
FT /id="VSP_026437"
FT VAR_SEQ 711..858
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19777325"
FT /id="VSP_026438"
FT VARIANT 562
FT /note="P -> L (in dbSNP:rs16837497)"
FT /evidence="ECO:0000269|PubMed:19777325"
FT /id="VAR_057464"
FT CONFLICT 118
FT /note="P -> A (in Ref. 1; AAX23974 and 3; AAZ30918)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="Q -> H (in Ref. 5; AAH73859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 89988 MW; 8C35F5685CF1E695 CRC64;
MDLPALLPAP TARGGQHGGG PGPLRRAPAP LGASPARRRL LLVRGPEDGG PGARPGEASG
PSPPPAEDDS DGDSFLVLLE VPHGGAAAEA AGSQEAEPGS RVNLASRPEQ GPSGPAAPPG
PGVAPAGAVT ISSQDLLVRL DRGVLALSAP PGPATAGAAA PRRAPQASGP STPGYRCPEP
QCALAFAKKH QLKVHLLTHG GGQGRRPFKC PLEGCGWAFT TSYKLKRHLQ SHDKLRPFGC
PVGGCGKKFT TVYNLKAHMK GHEQESLFKC EVCAERFPTH AKLSSHQRSH FEPERPYKCD
FPGCEKTFIT VSALFSHNRA HFREQELFSC SFPGCSKQYD KACRLKIHLR SHTGERPFIC
DSDSCGWTFT SMSKLLRHRR KHDDDRRFTC PVEGCGKSFT RAEHLKGHSI THLGTKPFEC
PVEGCCARFS ARSSLYIHSK KHVQDVGAPK SRCPVSTCNR LFTSKHSMKA HMVRQHSRRQ
DLLPQLEAPS SLTPSSELSS PGQSELTNMD LAALFSDTPA NASGSAGGSD EALNSGILTI
DVTSVSSSLG GNLPANNSSL GPMEPLVLVA HSDIPPSLDS PLVLGTAATV LQQGSFSVDD
VQTVSAGALG CLVALPMKNL SDDPLALTSN SNLAAHITTP TSSSTPRENA SVPELLAPIK
VEPDSPSRPG AVGQQEGSHG LPQSTLPSPA EQHGAQDTEL SAGTGNFYLE SGGSARTDYR
AIQLAKEKKQ RGAGSNAGAS QSTQRKIKEG KMSPPHFHAS QNSWLCGSLV VPSGGRPGPA
PAAGVQCGAQ GVQVQLVQDD PSGEGVLPSA RGPATFLPFL TVDLPVYVLQ EVLPSSGGPA
GPEATQFPGS TINLQDLQ
