ID APOL2_HUMAN Reviewed; 337 AA. AC Q9BQE5; B0QYK7; O95915; Q59GW9; Q5TH96; Q969T6; Q9BT28; Q9UGT1; Q9UH10; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 25-MAY-2022, sequence version 2. DT 27-MAR-2024, entry version 176. DE RecName: Full=Apolipoprotein L2; DE AltName: Full=Apolipoprotein L-II; DE Short=ApoL-II; GN Name=APOL2; 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]. RC TISSUE=Placenta; RX PubMed=11374903; DOI=10.1006/geno.2001.6534; RA Page N.M., Butlin D.J., Lomthaisong K., Lowry P.J.; RT "The human apolipoprotein L gene cluster: identification, classification, RT and sites of distribution."; RL Genomics 74:71-78(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Pancreas; RX PubMed=11290834; RA Duchateau P.N., Pullinger C.R., Cho M.H., Eng C., Kane J.P.; RT "Apolipoprotein L gene family: tissue-specific expression, splicing, RT promoter regions; discovery of a new gene."; RL J. Lipid Res. 42:620-630(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL LOCATION. RC TISSUE=Endothelial cell; RX PubMed=11944986; DOI=10.1006/geno.2002.6729; RA Monajemi H., Fontijn R.D., Pannekoek H., Horrevoets A.J.G.; RT "The apolipoprotein L gene cluster has emerged recently in evolution and is RT expressed in human vascular tissue."; RL Genomics 79:539-546(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Salivary gland; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [8] RP PROTEIN SEQUENCE OF 1-14; 249-259 AND 271-296, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, 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 [12] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS 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 [14] RP IDENTIFICATION BY 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: May affect the movement of lipids in the cytoplasm or allow CC the binding of lipids to organelles. CC -!- INTERACTION: CC Q9BQE5; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-4290634, EBI-11957045; CC Q9BQE5; P55056: APOC4; NbExp=3; IntAct=EBI-4290634, EBI-18302142; CC Q9BQE5; Q8WZ55: BSND; NbExp=3; IntAct=EBI-4290634, EBI-7996695; CC Q9BQE5; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-4290634, EBI-1045797; CC Q9BQE5; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-4290634, EBI-2680384; CC Q9BQE5; O00559: EBAG9; NbExp=3; IntAct=EBI-4290634, EBI-8787095; CC Q9BQE5; P54849: EMP1; NbExp=3; IntAct=EBI-4290634, EBI-4319440; CC Q9BQE5; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-4290634, EBI-781551; CC Q9BQE5; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-4290634, EBI-18304435; CC Q9BQE5; O00258: GET1; NbExp=3; IntAct=EBI-4290634, EBI-18908258; CC Q9BQE5; O95377: GJB5; NbExp=3; IntAct=EBI-4290634, EBI-3909454; CC Q9BQE5; P05107: ITGB2; NbExp=3; IntAct=EBI-4290634, EBI-300173; CC Q9BQE5; Q09470: KCNA1; NbExp=3; IntAct=EBI-4290634, EBI-8286599; CC Q9BQE5; Q86UD3: MARCHF3; NbExp=3; IntAct=EBI-4290634, EBI-2341065; CC Q9BQE5; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-4290634, EBI-11956541; CC Q9BQE5; O14880: MGST3; NbExp=3; IntAct=EBI-4290634, EBI-724754; CC Q9BQE5; Q96RD7: PANX1; NbExp=3; IntAct=EBI-4290634, EBI-7037612; CC Q9BQE5; Q8TD22: SFXN5; NbExp=3; IntAct=EBI-4290634, EBI-17274136; CC Q9BQE5; Q9Y3P8: SIT1; NbExp=3; IntAct=EBI-4290634, EBI-6977215; CC Q9BQE5; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-4290634, EBI-17595455; CC Q9BQE5; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-4290634, EBI-12814225; CC Q9BQE5; Q16623: STX1A; NbExp=3; IntAct=EBI-4290634, EBI-712466; CC Q9BQE5; P32856-2: STX2; NbExp=3; IntAct=EBI-4290634, EBI-11956649; CC Q9BQE5; Q6PL24: TMED8; NbExp=3; IntAct=EBI-4290634, EBI-11603430; CC Q9BQE5; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-4290634, EBI-7238458; CC Q9BQE5; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-4290634, EBI-11724423; CC Q9BQE5; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-4290634, EBI-3923061; CC Q9BQE5; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-4290634, EBI-18178701; CC Q9BQE5; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-4290634, EBI-2852148; CC Q9BQE5; Q9NZ43: USE1; NbExp=3; IntAct=EBI-4290634, EBI-742842; CC Q9BQE5; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-4290634, EBI-751210; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Widely expressed; the highest levels are found in CC lung, thymus, pancreas, placenta, adult brain and prostate; also CC detected in spleen, liver, kidney, colon, small intestine, uterus, CC spinal cord, adrenal gland, salivary gland, trachea, mammary gland, CC skeletal muscle, testis and fetal brain and liver. CC -!- SIMILARITY: Belongs to the apolipoprotein L family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92227.1; Type=Erroneous initiation; 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; AF305225; AAK20211.1; -; mRNA. DR EMBL; AF324223; AAK11592.1; -; mRNA. DR EMBL; AF324224; AAK11593.1; -; mRNA. DR EMBL; AF324230; AAK11598.1; -; Genomic_DNA. DR EMBL; AF324228; AAK11598.1; JOINED; Genomic_DNA. DR EMBL; AF324229; AAK11598.1; JOINED; Genomic_DNA. DR EMBL; AF305429; AAL09359.1; -; mRNA. DR EMBL; AK056938; BAB71315.1; -; mRNA. DR EMBL; AB208990; BAD92227.1; ALT_INIT; mRNA. DR EMBL; AL031426; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z82215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z95114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004395; AAH04395.1; -; mRNA. DR CCDS; CCDS43014.1; -. DR RefSeq; NP_112092.2; NM_030882.3. DR RefSeq; NP_663612.2; NM_145637.2. DR RefSeq; XP_011528376.1; XM_011530074.1. DR RefSeq; XP_011528377.1; XM_011530075.1. DR RefSeq; XP_011528378.1; XM_011530076.2. DR RefSeq; XP_011528379.1; XM_011530077.2. DR RefSeq; XP_011528380.1; XM_011530078.1. DR PDB; 7LF8; X-ray; 2.15 A; A=2-113. DR PDBsum; 7LF8; -. DR AlphaFoldDB; Q9BQE5; -. DR SMR; Q9BQE5; -. DR BioGRID; 117279; 109. DR IntAct; Q9BQE5; 60. DR STRING; 9606.ENSP00000249066; -. DR iPTMnet; Q9BQE5; -. DR MetOSite; Q9BQE5; -. DR PhosphoSitePlus; Q9BQE5; -. DR BioMuta; APOL2; -. DR DMDM; 17433285; -. DR EPD; Q9BQE5; -. DR jPOST; Q9BQE5; -. DR MassIVE; Q9BQE5; -. DR MaxQB; Q9BQE5; -. DR PaxDb; 9606-ENSP00000249066; -. DR PeptideAtlas; Q9BQE5; -. DR ProteomicsDB; 78663; -. DR Pumba; Q9BQE5; -. DR Antibodypedia; 25557; 228 antibodies from 34 providers. DR DNASU; 23780; -. DR Ensembl; ENST00000249066.10; ENSP00000249066.6; ENSG00000128335.14. DR Ensembl; ENST00000358502.10; ENSP00000351292.5; ENSG00000128335.14. DR GeneID; 23780; -. DR KEGG; hsa:23780; -. DR MANE-Select; ENST00000358502.10; ENSP00000351292.5; NM_030882.4; NP_112092.2. DR UCSC; uc003aoz.4; human. DR AGR; HGNC:619; -. DR CTD; 23780; -. DR DisGeNET; 23780; -. DR GeneCards; APOL2; -. DR HGNC; HGNC:619; APOL2. DR HPA; ENSG00000128335; Low tissue specificity. DR MalaCards; APOL2; -. DR MIM; 607252; gene. DR neXtProt; NX_Q9BQE5; -. DR OpenTargets; ENSG00000128335; -. DR PharmGKB; PA24905; -. DR VEuPathDB; HostDB:ENSG00000128335; -. DR eggNOG; ENOG502RZGU; Eukaryota. DR GeneTree; ENSGT01030000234599; -. DR HOGENOM; CLU_046288_1_0_1; -. DR InParanoid; Q9BQE5; -. DR OMA; FIGKFHE; -. DR OrthoDB; 5323587at2759; -. DR PhylomeDB; Q9BQE5; -. DR TreeFam; TF334681; -. DR PathwayCommons; Q9BQE5; -. DR SignaLink; Q9BQE5; -. DR BioGRID-ORCS; 23780; 15 hits in 1159 CRISPR screens. DR ChiTaRS; APOL2; human. DR GeneWiki; APOL2; -. DR GenomeRNAi; 23780; -. DR Pharos; Q9BQE5; Tbio. DR PRO; PR:Q9BQE5; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9BQE5; Protein. DR Bgee; ENSG00000128335; Expressed in tendon of biceps brachii and 198 other cell types or tissues. DR ExpressionAtlas; Q9BQE5; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008035; F:high-density lipoprotein particle binding; NAS:UniProtKB. DR GO; GO:0008289; F:lipid binding; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; NAS:UniProtKB. DR GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; NAS:UniProtKB. DR GO; GO:0006869; P:lipid transport; NAS:UniProtKB. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR GO; GO:0060135; P:maternal process involved in female pregnancy; NAS:UniProtKB. DR InterPro; IPR008405; ApoL. DR PANTHER; PTHR14096; APOLIPOPROTEIN L; 1. DR PANTHER; PTHR14096:SF27; APOLIPOPROTEIN L2; 1. DR Pfam; PF05461; ApoL; 1. DR Genevisible; Q9BQE5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Lipid transport; Phosphoprotein; Reference proteome; Transport. FT CHAIN 1..337 FT /note="Apolipoprotein L2" FT /id="PRO_0000137601" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231" FT VARIANT 182 FT /note="R -> C (in dbSNP:rs7285167)" FT /id="VAR_024366" FT VARIANT 245 FT /note="V -> I (in dbSNP:rs132760)" FT /id="VAR_012978" FT CONFLICT 186 FT /note="Q -> R (in Ref. 5; BAD92227)" FT /evidence="ECO:0000305" FT HELIX 7..19 FT /evidence="ECO:0007829|PDB:7LF8" FT HELIX 22..30 FT /evidence="ECO:0007829|PDB:7LF8" FT HELIX 32..42 FT /evidence="ECO:0007829|PDB:7LF8" FT HELIX 46..61 FT /evidence="ECO:0007829|PDB:7LF8" SQ SEQUENCE 337 AA; 37078 MW; 81D7CF9FD2ED8AF1 CRC64; MNPESSIFIE DYLKYFQDQV SRENLLQLLT DDEAWNGFVA AAELPRDEAD ELRKALNKLA SHMVMKDKNR HDKDQQHRQW FLKEFPRLKR ELEDHIRKLR ALAEEVEQVH RGTTIANVVS NSVGTTSGIL TLLGLGLAPF TEGISFVLLD TGMGLGAAAA VAGITCSVVE LVNKLRARAQ ARNLDQSGTN VAKVMKEFVG GNTPNVLTLV DNWYQVTQGI GRNIRAIRRA RANPQLGAYA PPPHVIGRIS AEGGEQVERV VEGPAQAMSR GTMIVGAATG GILLLLDVVS LAYESKHLLE GAKSESAEEL KKRAQELEGK LNFLTKIHEM LQPGQDQ //