PUM3_HUMAN
ID PUM3_HUMAN Reviewed; 648 AA.
AC Q15397; A8K804; Q547G7; Q5SZY9; Q6IB47; Q96B27; Q96L78; Q96L79; Q96L80;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Pumilio homolog 3 {ECO:0000305};
DE AltName: Full=HBV X-transactivated gene 5 protein;
DE AltName: Full=HBV XAg-transactivated protein 5;
DE AltName: Full=Minor histocompatibility antigen HA-8;
DE Short=HLA-HA8;
GN Name=PUM3 {ECO:0000312|HGNC:HGNC:29676};
GN Synonyms=cPERP-C {ECO:0000303|PubMed:20813266},
GN KIAA0020 {ECO:0000312|HGNC:HGNC:29676},
GN PUF-A {ECO:0000303|PubMed:21266351}, XTP5;
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].
RC TISSUE=Synovium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE HA-8R).
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 [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE HA-8PL), AND VARIANT ASN-13.
RC TISSUE=Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-648 (ALLELE HA-8R), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [6]
RP PROTEIN SEQUENCE OF 130-137; 294-301; 331-342; 345-352 AND 441-464,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 141-648 (ALLELE HA-8R).
RA Liu Y., Cheng J., Lu Y., Wang G., Li K., Chen J., Li L.;
RT "Cloning and identification of human gene 5 transactivated by hepatitis B
RT virus X antigen.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-648 (ALLELE HA-8R).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-350 (ALLELES HA-8R; HA-8P AND HA-8PL),
RP IDENTIFICATION BY MASS SPECTROMETRY OF HA-8, AND POLYMORPHISM.
RC TISSUE=B-cell;
RX PubMed=11148223; DOI=10.1084/jem.193.2.195;
RA Brickner A.G., Warren E.H., Caldwell J.A., Akatsuka Y., Golovina T.N.,
RA Zarling A.L., Shabanowitz J., Eisenlohr L.C., Hunt D.F., Engelhard V.H.,
RA Riddell S.R.;
RT "The immunogenicity of a new human minor histocompatibility antigen results
RT from differential antigen processing.";
RL J. Exp. Med. 193:195-206(2001).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [12]
RP FUNCTION, INTERACTION WITH PARP1, SUBCELLULAR LOCATION, AND NUCLEAR
RP LOCALIZATION SIGNAL.
RX PubMed=21266351; DOI=10.1158/0008-5472.can-10-1831;
RA Chang H.Y., Fan C.C., Chu P.C., Hong B.E., Lee H.J., Chang M.S.;
RT "hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress.";
RL Cancer Res. 71:1126-1134(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 123-648 ALONE AND IN COMPLEX WITH
RP DOUBLE-STRANDED DNA, PUMILIO REPEATS, RNA-BINDING, AND DNA-BINDING.
RX PubMed=25512524; DOI=10.1073/pnas.1407634112;
RA Qiu C., McCann K.L., Wine R.N., Baserga S.J., Hall T.M.;
RT "A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA
RT localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:18554-18559(2014).
CC -!- FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the
CC degradation of PARP1 by CASP3 following genotoxic stress
CC (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence
CC specificity (PubMed:25512524). Involved in development of the eye and
CC of primordial germ cells (By similarity).
CC {ECO:0000250|UniProtKB:X1WGX5, ECO:0000269|PubMed:21266351,
CC ECO:0000269|PubMed:25512524}.
CC -!- SUBUNIT: Interacts with PARP1 (via catalytic domain).
CC {ECO:0000269|PubMed:21266351}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:21266351, ECO:0000269|Ref.6}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:21266351}. Chromosome
CC {ECO:0000269|PubMed:20813266}. Note=Localizes predominantly in the
CC nucleolus with minor punctate signals in the nucleoplasm.
CC {ECO:0000269|PubMed:21266351}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7584026}.
CC -!- DOMAIN: The HA-8 region can be cleaved and exposed at the cell surface
CC where it plays a role as a minor histocompatibility HLA-A*0201-
CC restricted antigen.
CC -!- DOMAIN: A 90 degree bend between Pumilio repeats 3 and 4 gives rise to
CC a L-shaped protein. {ECO:0000269|PubMed:25512524}.
CC -!- POLYMORPHISM: The following alleles of HA-8 are known: HA-8R, HA-8P,
CC HA-8PL, of which only HA-8R leads to specific cytotoxic T lymphocyte
CC (CTL) recognition. The lack of CTL recognition of cells expressing HA-
CC 8P may be due to impaired transport associated with antigen processing.
CC The sequence shown is that of HA-8R. {ECO:0000269|PubMed:11148223}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02808.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK292169; BAF84858.1; -; mRNA.
DR EMBL; AL354723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58802.1; -; Genomic_DNA.
DR EMBL; BC016137; AAH16137.2; -; mRNA.
DR EMBL; D13645; BAA02808.1; ALT_INIT; mRNA.
DR EMBL; AF490254; AAO85462.1; -; mRNA.
DR EMBL; CR456957; CAG33238.1; -; mRNA.
DR EMBL; AY047588; AAL06072.1; -; mRNA.
DR EMBL; AY047589; AAL06073.1; -; mRNA.
DR EMBL; AY047590; AAL06074.1; -; mRNA.
DR CCDS; CCDS6448.2; -.
DR RefSeq; NP_055693.4; NM_014878.4.
DR PDB; 4WZR; X-ray; 2.15 A; A/B=123-648.
DR PDB; 4WZW; X-ray; 2.95 A; A=129-648.
DR PDBsum; 4WZR; -.
DR PDBsum; 4WZW; -.
DR AlphaFoldDB; Q15397; -.
DR SMR; Q15397; -.
DR BioGRID; 115259; 249.
DR IntAct; Q15397; 114.
DR MINT; Q15397; -.
DR STRING; 9606.ENSP00000380982; -.
DR iPTMnet; Q15397; -.
DR PhosphoSitePlus; Q15397; -.
DR SwissPalm; Q15397; -.
DR BioMuta; PUM3; -.
DR DMDM; 81175177; -.
DR SWISS-2DPAGE; Q15397; -.
DR EPD; Q15397; -.
DR jPOST; Q15397; -.
DR MassIVE; Q15397; -.
DR MaxQB; Q15397; -.
DR PaxDb; Q15397; -.
DR PeptideAtlas; Q15397; -.
DR PRIDE; Q15397; -.
DR ProteomicsDB; 60566; -.
DR Antibodypedia; 1036; 113 antibodies from 21 providers.
DR DNASU; 9933; -.
DR Ensembl; ENST00000397885.3; ENSP00000380982.2; ENSG00000080608.10.
DR GeneID; 9933; -.
DR KEGG; hsa:9933; -.
DR MANE-Select; ENST00000397885.3; ENSP00000380982.2; NM_014878.5; NP_055693.4.
DR UCSC; uc003zhp.2; human.
DR CTD; 9933; -.
DR DisGeNET; 9933; -.
DR GeneCards; PUM3; -.
DR HGNC; HGNC:29676; PUM3.
DR HPA; ENSG00000080608; Low tissue specificity.
DR MIM; 609960; gene.
DR neXtProt; NX_Q15397; -.
DR OpenTargets; ENSG00000080608; -.
DR PharmGKB; PA134895115; -.
DR VEuPathDB; HostDB:ENSG00000080608; -.
DR eggNOG; KOG2050; Eukaryota.
DR GeneTree; ENSGT00390000015757; -.
DR HOGENOM; CLU_013994_0_1_1; -.
DR InParanoid; Q15397; -.
DR OMA; WILDDVY; -.
DR OrthoDB; 845051at2759; -.
DR PhylomeDB; Q15397; -.
DR TreeFam; TF312954; -.
DR PathwayCommons; Q15397; -.
DR SignaLink; Q15397; -.
DR SIGNOR; Q15397; -.
DR BioGRID-ORCS; 9933; 65 hits in 1075 CRISPR screens.
DR ChiTaRS; PUM3; human.
DR GeneWiki; KIAA0020; -.
DR GenomeRNAi; 9933; -.
DR Pharos; Q15397; Tbio.
DR PRO; PR:Q15397; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15397; protein.
DR Bgee; ENSG00000080608; Expressed in adrenal tissue and 180 other tissues.
DR ExpressionAtlas; Q15397; baseline and differential.
DR Genevisible; Q15397; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IMP:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012959; CPL_dom.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR040059; PUM3.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR PANTHER; PTHR13389; PTHR13389; 1.
DR Pfam; PF08144; CPL; 1.
DR SMART; SM00025; Pumilio; 6.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50302; PUM; 5.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing;
KW DNA-binding; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..648
FT /note="Pumilio homolog 3"
FT /id="PRO_0000075929"
FT DOMAIN 143..510
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 177..212
FT /note="Pumilio 1"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 213..248
FT /note="Pumilio 2"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 249..277
FT /note="Pumilio 3"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 289..325
FT /note="Pumilio 4"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 326..361
FT /note="Pumilio 5"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 362..397
FT /note="Pumilio 6"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 398..435
FT /note="Pumilio 7"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 436..504
FT /note="Pumilio 8"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 505..551
FT /note="Pumilio 9"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 552..596
FT /note="Pumilio 10"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REPEAT 597..636
FT /note="Pumilio 11"
FT /evidence="ECO:0000269|PubMed:25512524"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..297
FT /note="HA-8"
FT MOTIF 106..118
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21266351"
FT COMPBIAS 90..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKS9"
FT VARIANT 13
FT /note="S -> N (in dbSNP:rs10968457)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051613"
FT VARIANT 264
FT /note="I -> V (in dbSNP:rs35869387)"
FT /id="VAR_051614"
FT VARIANT 289
FT /note="R -> P (in allele HA-8P and allele HA-8PL;
FT dbSNP:rs2173904)"
FT /evidence="ECO:0000269|PubMed:11148223,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023772"
FT VARIANT 297
FT /note="V -> L (in allele HA-8PL; dbSNP:rs2270891)"
FT /evidence="ECO:0000269|PubMed:11148223,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023773"
FT VARIANT 414
FT /note="T -> S (in dbSNP:rs3736390)"
FT /id="VAR_051615"
FT VARIANT 480
FT /note="R -> Q (in dbSNP:rs2270889)"
FT /id="VAR_051616"
FT CONFLICT 625
FT /note="L -> S (in Ref. 8; CAG33238)"
FT /evidence="ECO:0000305"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:4WZR"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:4WZR"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 456..463
FT /evidence="ECO:0007829|PDB:4WZR"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 475..496
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 554..570
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 577..585
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 597..607
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 612..622
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 626..629
FT /evidence="ECO:0007829|PDB:4WZR"
FT HELIX 637..645
FT /evidence="ECO:0007829|PDB:4WZR"
SQ SEQUENCE 648 AA; 73584 MW; 449BFBF22F1BBA86 CRC64;
MEVKGKKQFT GKSTKTAQEK NRFHKNSDSG SSKTFPTRKV AKEGGPKVTS RNFEKSITKL
GKKGVKQFKN KQQGDKSPKN KFQPANKFNK KRKFQPDGRS DESAAKKPKW DDFKKKKKEL
KQSRQLSDKT NYDIVVRAKQ MWEILRRKDC DKEKRVKLMS DLQKLIQGKI KTIAFAHDST
RVIQCYIQYG NEEQRKQAFE ELRDDLVELS KAKYSRNIVK KFLMYGSKPQ IAEIIRSFKG
HVRKMLRHAE ASAIVEYAYN DKAILEQRNM LTEELYGNTF QLYKSADHRT LDKVLEVQPE
KLELIMDEMK QILTPMAQKE AVIKHSLVHK VFLDFFTYAP PKLRSEMIEA IREAVVYLAH
THDGARVAMH CLWHGTPKDR KVIVKTMKTY VEKVANGQYS HLVLLAAFDC IDDTKLVKQI
IISEIISSLP SIVNDKYGRK VLLYLLSPRD PAHTVREIIE VLQKGDGNAH SKKDTEVRRR
ELLESISPAL LSYLQEHAQE VVLDKSACVL VSDILGSATG DVQPTMNAIA SLAATGLHPG
GKDGELHIAE HPAGHLVLKW LIEQDKKMKE NGREGCFAKT LVEHVGMKNL KSWASVNRGA
IILSSLLQSC DLEVANKVKA ALKSLIPTLE KTKSTSKGIE ILLEKLST
