APOL2_HUMAN
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 03-AUG-2022, entry version 167.
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};
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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; 102.
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; Q9BQE5; -.
DR PeptideAtlas; Q9BQE5; -.
DR PRIDE; Q9BQE5; -.
DR ProteomicsDB; 78663; -.
DR Antibodypedia; 25557; 211 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 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 PhylomeDB; Q9BQE5; -.
DR TreeFam; TF334681; -.
DR PathwayCommons; Q9BQE5; -.
DR SignaLink; Q9BQE5; -.
DR BioGRID-ORCS; 23780; 8 hits in 1079 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 196 other tissues.
DR ExpressionAtlas; Q9BQE5; baseline and differential.
DR Genevisible; Q9BQE5; HS.
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; PTHR14096; 1.
DR Pfam; PF05461; ApoL; 1.
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"
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
