ID S39AA_HUMAN Reviewed; 831 AA. AC Q9ULF5; A8K5C6; B4DGU0; Q3MJA4; Q68CR5; Q6DKH6; Q9Y3Z1; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 2. DT 27-MAR-2024, entry version 156. DE RecName: Full=Zinc transporter ZIP10 {ECO:0000305}; DE AltName: Full=Solute carrier family 39 member 10; DE AltName: Full=Zrt- and Irt-like protein 10; DE Short=ZIP-10; DE Flags: Precursor; GN Name=SLC39A10 {ECO:0000312|HGNC:HGNC:20861}; Synonyms=KIAA1265, ZIP10; 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=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 MRNA] (ISOFORM 1). RC TISSUE=Brain, and Colon carcinoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, 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 FUNCTION, TRANSPORTER ACTIVITY, AND INDUCTION. RX PubMed=17359283; DOI=10.1111/j.1349-7006.2007.00446.x; RA Kagara N., Tanaka N., Noguchi S., Hirano T.; RT "Zinc and its transporter ZIP10 are involved in invasive behavior of breast RT cancer cells."; RL Cancer Sci. 98:692-697(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-553, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-536 AND SER-591, AND RP IDENTIFICATION BY 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-591, AND IDENTIFICATION BY RP 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 [11] RP SUBCELLULAR LOCATION, FUNCTION, TRANSPORTER ACTIVITY, INDUCTION, AND RP INTERACTION WITH SLC39A6. RX PubMed=27274087; DOI=10.1042/bcj20160388; RA Taylor K.M., Muraina I.A., Brethour D., Schmitt-Ulms G., Nimmanon T., RA Ziliotto S., Kille P., Hogstrand C.; RT "Zinc transporter ZIP10 forms a heteromer with ZIP6 which regulates RT embryonic development and cell migration."; RL Biochem. J. 473:2531-2544(2016). RN [12] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=30520657; DOI=10.1152/ajprenal.00573.2017; RA Landry G.M., Furrow E., Holmes H.L., Hirata T., Kato A., Williams P., RA Strohmaier K., Gallo C.J.R., Chang M., Pandey M.K., Jiang H., Bansal A., RA Franz M.C., Montalbetti N., Alexander M.P., Cabrero P., Dow J.A.T., RA DeGrado T.R., Romero M.F.; RT "Cloning, function, and localization of human, canine, and Drosophila ZIP10 RT (SLC39A10), a Zn2+ transporter."; RL Am. J. Physiol. 316:F263-F273(2019). RN [13] RP SUBUNIT, FUNCTION, IDENTIFICATION IN A COMPLEX WITH SLC39A10 AND STAT3, AND RP PROTEOLYTIC CLEAVAGE. RX PubMed=32797246; DOI=10.1007/s00018-020-03616-6; RA Nimmanon T., Ziliotto S., Ogle O., Burt A., Gee J.M.W., Andrews G.K., RA Kille P., Hogstrand C., Maret W., Taylor K.M.; RT "The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of RT mitosis."; RL Cell. Mol. Life Sci. 78:1781-1798(2021). CC -!- FUNCTION: Zinc-influx transporter (PubMed:30520657, PubMed:17359283, CC PubMed:27274087). When associated with SLC39A6, the heterodimer formed CC by SLC39A10 and SLC39A6 mediates cellular zinc uptake to trigger cells CC to undergo epithelial-to-mesenchymal transition (EMT) CC (PubMed:23186163). SLC39A10-SLC39A6 heterodimers play also an essentiel CC role in initiating mitosis by importing zinc into cells to initiate a CC pathway resulting in the onset of mitosis (PubMed:32797246). Plays an CC important for both mature B-cell maintenance and humoral immune CC responses (By similarity). When associated with SLC39A10, the CC heterodimer controls NCAM1 phosphorylation and integration into focal CC adhesion complexes during EMT (By similarity). CC {ECO:0000250|UniProtKB:Q6P5F6, ECO:0000269|PubMed:17359283, CC ECO:0000269|PubMed:23186163, ECO:0000269|PubMed:27274087, CC ECO:0000269|PubMed:30520657, ECO:0000269|PubMed:32797246}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, CC ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17359283, CC ECO:0000269|PubMed:27274087, ECO:0000269|PubMed:30520657}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29353; CC Evidence={ECO:0000305|PubMed:30520657}; CC -!- SUBUNIT: Interacts with SLC39A6; which triggers cells to undergo EMT CC and mitosis (PubMed:27274087, PubMed:32797246). Found in a complex with CC SLC39A6, SLC39A10 and with the 'Ser-727' phosphorylated form of STAT3 CC throughout mitosis (PubMed:32797246). Found in a complex with SLC39A6, CC SLC39A10 and with NCAM1; this complex controls NCAM1 phosphorylation CC and integration into focal adhesion complexes during epithelial- CC tomesenchymal transition. Found in a complex with SLC39A6, SLC39A10 and CC with GSK3B that controls NCAM1 phosphorylation (By similarity). CC {ECO:0000250|UniProtKB:Q6P5F6, ECO:0000269|PubMed:27274087, CC ECO:0000269|PubMed:32797246}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27274087}; CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane CC {ECO:0000269|PubMed:30520657}; Multi-pass membrane protein CC {ECO:0000255}. Note=Expressed at the apical membranes of proximal CC tubules in the kidney. {ECO:0000269|PubMed:30520657}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9ULF5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ULF5-2; Sequence=VSP_055991; CC -!- INDUCTION: Up-regulated in several breast cancer lines, and correlated CC to cancer progression as a marker of metastatic breast cancer. CC {ECO:0000269|PubMed:17359283, ECO:0000269|PubMed:27274087}. CC -!- PTM: Undergoes N-terminal ectodomain shedding. CC {ECO:0000269|PubMed:32797246}. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86579.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAB43393.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; AB033091; BAA86579.1; ALT_INIT; mRNA. DR EMBL; AK291241; BAF83930.1; -; mRNA. DR EMBL; AK294771; BAG57901.1; -; mRNA. DR EMBL; AL050294; CAB43393.1; ALT_SEQ; mRNA. DR EMBL; CR749813; CAH18673.1; -; mRNA. DR EMBL; AC013274; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC064834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70116.1; -; Genomic_DNA. DR EMBL; BC073909; AAH73909.1; -; mRNA. DR EMBL; BC101516; AAI01517.1; -; mRNA. DR EMBL; BC112223; AAI12224.1; -; mRNA. DR CCDS; CCDS33353.1; -. [Q9ULF5-1] DR PIR; T08684; T08684. DR RefSeq; NP_001120729.1; NM_001127257.1. [Q9ULF5-1] DR RefSeq; NP_065075.1; NM_020342.2. [Q9ULF5-1] DR RefSeq; XP_005246746.2; XM_005246689.4. DR RefSeq; XP_011509806.1; XM_011511504.2. [Q9ULF5-1] DR RefSeq; XP_011509807.1; XM_011511505.2. DR RefSeq; XP_011509808.1; XM_011511506.2. DR AlphaFoldDB; Q9ULF5; -. DR BioGRID; 121430; 197. DR IntAct; Q9ULF5; 45. DR MINT; Q9ULF5; -. DR STRING; 9606.ENSP00000386766; -. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR TCDB; 2.A.5.4.6; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family. DR GlyCosmos; Q9ULF5; 4 sites, No reported glycans. DR GlyGen; Q9ULF5; 11 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q9ULF5; -. DR PhosphoSitePlus; Q9ULF5; -. DR SwissPalm; Q9ULF5; -. DR BioMuta; SLC39A10; -. DR DMDM; 156630627; -. DR EPD; Q9ULF5; -. DR jPOST; Q9ULF5; -. DR MassIVE; Q9ULF5; -. DR MaxQB; Q9ULF5; -. DR PaxDb; 9606-ENSP00000386766; -. DR PeptideAtlas; Q9ULF5; -. DR ProteomicsDB; 4160; -. DR ProteomicsDB; 85012; -. [Q9ULF5-1] DR Pumba; Q9ULF5; -. DR Antibodypedia; 34052; 158 antibodies from 28 providers. DR DNASU; 57181; -. DR Ensembl; ENST00000359634.10; ENSP00000352655.5; ENSG00000196950.14. [Q9ULF5-1] DR Ensembl; ENST00000409086.7; ENSP00000386766.3; ENSG00000196950.14. [Q9ULF5-1] DR GeneID; 57181; -. DR KEGG; hsa:57181; -. DR MANE-Select; ENST00000359634.10; ENSP00000352655.5; NM_020342.3; NP_065075.1. DR UCSC; uc002utg.5; human. [Q9ULF5-1] DR AGR; HGNC:20861; -. DR CTD; 57181; -. DR DisGeNET; 57181; -. DR GeneCards; SLC39A10; -. DR HGNC; HGNC:20861; SLC39A10. DR HPA; ENSG00000196950; Tissue enhanced (brain, thyroid gland). DR MIM; 608733; gene. DR neXtProt; NX_Q9ULF5; -. DR OpenTargets; ENSG00000196950; -. DR PharmGKB; PA134944068; -. DR VEuPathDB; HostDB:ENSG00000196950; -. DR eggNOG; KOG2693; Eukaryota. DR GeneTree; ENSGT00940000160335; -. DR HOGENOM; CLU_015114_13_2_1; -. DR InParanoid; Q9ULF5; -. DR OMA; HATAHNH; -. DR OrthoDB; 5488029at2759; -. DR PhylomeDB; Q9ULF5; -. DR TreeFam; TF318470; -. DR PathwayCommons; Q9ULF5; -. DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family. DR SignaLink; Q9ULF5; -. DR BioGRID-ORCS; 57181; 258 hits in 1164 CRISPR screens. DR ChiTaRS; SLC39A10; human. DR GeneWiki; SLC39A10; -. DR GenomeRNAi; 57181; -. DR Pharos; Q9ULF5; Tbio. DR PRO; PR:Q9ULF5; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9ULF5; Protein. DR Bgee; ENSG00000196950; Expressed in middle temporal gyrus and 179 other cell types or tissues. DR ExpressionAtlas; Q9ULF5; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0140410; F:monoatomic cation:bicarbonate symporter activity; IBA:GO_Central. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:Ensembl. DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IEA:Ensembl. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl. DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0071578; P:zinc ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:UniProtKB. DR InterPro; IPR003689; ZIP. DR PANTHER; PTHR12191; SOLUTE CARRIER FAMILY 39; 1. DR PANTHER; PTHR12191:SF14; ZINC TRANSPORTER ZIP10; 1. DR Pfam; PF02535; Zip; 1. DR Genevisible; Q9ULF5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport; Zinc; Zinc transport. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..831 FT /note="Zinc transporter ZIP10" FT /id="PRO_0000297632" FT TRANSMEM 411..431 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 438..458 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 495..515 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 687..707 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 732..752 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 759..779 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 801..821 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 126..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 464..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 134..148 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..173 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 174..191 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 203..222 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..316 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 536 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 553 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 591 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 198 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 218 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 339 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..450 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055991" FT VARIANT 87 FT /note="T -> S (in dbSNP:rs13419724)" FT /id="VAR_034658" FT CONFLICT 426 FT /note="I -> T (in Ref. 3; CAB43393/CAH18673)" FT /evidence="ECO:0000305" SQ SEQUENCE 831 AA; 94132 MW; E196111D12BC20ED CRC64; MKVHMHTKFC LICLLTFIFH HCNHCHEEHD HGPEALHRQH RGMTELEPSK FSKQAAENEK KYYIEKLFER YGENGRLSFF GLEKLLTNLG LGERKVVEIN HEDLGHDHVS HLDILAVQEG KHFHSHNHQH SHNHLNSENQ TVTSVSTKRN HKCDPEKETV EVSVKSDDKH MHDHNHRLRH HHRLHHHLDH NNTHHFHNDS ITPSERGEPS NEPSTETNKT QEQSDVKLPK GKRKKKGRKS NENSEVITPG FPPNHDQGEQ YEHNRVHKPD RVHNPGHSHV HLPERNGHDP GRGHQDLDPD NEGELRHTRK REAPHVKNNA IISLRKDLNE DDHHHECLNV TQLLKYYGHG ANSPISTDLF TYLCPALLYQ IDSRLCIEHF DKLLVEDINK DKNLVPEDEA NIGASAWICG IISITVISLL SLLGVILVPI INQGCFKFLL TFLVALAVGT MSGDALLHLL PHSQGGHDHS HQHAHGHGHS HGHESNKFLE EYDAVLKGLV ALGGIYLLFI IEHCIRMFKH YKQQRGKQKW FMKQNTEEST IGRKLSDHKL NNTPDSDWLQ LKPLAGTDDS VVSEDRLNET ELTDLEGQQE SPPKNYLCIE EEKIIDHSHS DGLHTIHEHD LHAAAHNHHG ENKTVLRKHN HQWHHKHSHH SHGPCHSGSD LKETGIANIA WMVIMGDGIH NFSDGLAIGA AFSAGLTGGI STSIAVFCHE LPHELGDFAV LLKAGMTVKQ AIVYNLLSAM MAYIGMLIGT AVGQYANNIT LWIFAVTAGM FLYVALVDML PEMLHGDGDN EEHGFCPVGQ FILQNLGLLF GFAIMLVIAL YEDKIVFDIQ F //