PAIP1_HUMAN
ID PAIP1_HUMAN Reviewed; 479 AA.
AC Q9H074; A6NKV8; O60455; Q96B61; Q9BS63;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 1 {ECO:0000305};
DE Short=PABP-interacting protein 1;
DE Short=PAIP-1;
DE Short=Poly(A)-binding protein-interacting protein 1;
GN Name=PAIP1 {ECO:0000312|HGNC:HGNC:16945};
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 IN TRANSLATION INITIATION
RP STIMULATION, AND INTERACTION WITH PABPC1 AND EIF4A.
RC TISSUE=Placenta;
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP
RT enhances translation.";
RL Nature 392:520-523(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Skin;
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 1-249 (ISOFORM 3).
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 FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION IN A
RP COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND UNR.
RX PubMed=11051545; DOI=10.1016/s0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction between
RT the poly(A) tail and a c-fos RNA coding determinant via a protein
RT complex.";
RL Cell 103:29-40(2000).
RN [7]
RP INTERACTION WITH PABPC1.
RX PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
RA Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
RT "Multiple portions of poly(A)-binding protein stimulate translation in
RT vivo.";
RL EMBO J. 19:4723-4733(2000).
RN [8]
RP INTERACTION WITH PABPC1.
RX PubMed=11172725; DOI=10.1016/s1097-2765(01)00168-x;
RA Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
RA Burley S.K., Sonenberg N.;
RT "Translational repression by a novel partner of human poly(A) binding
RT protein, Paip2.";
RL Mol. Cell 7:205-216(2001).
RN [9]
RP INTERACTION WITH PABPC1.
RX PubMed=11997512; DOI=10.1128/mcb.22.11.3769-3782.2002;
RA Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M.,
RA Sonenberg N.;
RT "Paip1 interacts with poly(A) binding protein through two independent
RT binding motifs.";
RL Mol. Cell. Biol. 22:3769-3782(2002).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 3), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 157-375 IN COMPLEX WITH SARS-COV
RP NSP3 PROTEIN, INTERACTION WITH SARS-COV AND SARS-COV2 NSP3 PROTEIN
RP (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH
RP PABPC1.
RX PubMed=33876849; DOI=10.15252/embj.2019102277;
RA Lei J., Ma-Lauer Y., Han Y., Thoms M., Buschauer R., Jores J., Thiel V.,
RA Beckmann R., Deng W., Leonhardt H., Hilgenfeld R., von Brunn A.;
RT "The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with
RT human Paip1 to enhance viral RNA translation.";
RL EMBO J. 40:e102277-e102277(2021).
CC -!- FUNCTION: Acts as a coactivator in the regulation of translation
CC initiation of poly(A)-containing mRNAs. Its stimulatory activity on
CC translation is mediated via its action on PABPC1. Competes with PAIP2
CC for binding to PABPC1. Its association with EIF4A and PABPC1 may
CC potentiate contacts between mRNA termini. May also be involved in
CC translationally coupled mRNA turnover. Implicated with other RNA-
CC binding proteins in the cytoplasmic deadenylation/translational and
CC decay interplay of the FOS mRNA mediated by the major coding-region
CC determinant of instability (mCRD) domain. {ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:9548260}.
CC -!- FUNCTION: (Microbial infection) Upon interaction with SARS coronavirus
CC SARS-CoV NSP3 protein, plays an important role in viral protein
CC synthesis. {ECO:0000269|PubMed:33876849}.
CC -!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of PABPC1
CC in a 1:1 stoichiometry. Interacts with EIF4A.
CC {ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:11172725, ECO:0000269|PubMed:11997512,
CC ECO:0000269|PubMed:33876849, ECO:0000269|PubMed:9548260}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via PAIP1M) with human SARS
CC coronaviruses SARS-COV and SARS-COV-2 NSP3 protein (via SARS-unique
CC domain); the interaction increases binding affinity with PABPC1.
CC {ECO:0000269|PubMed:33876849}.
CC -!- INTERACTION:
CC Q9H074; P11940: PABPC1; NbExp=16; IntAct=EBI-81519, EBI-81531;
CC Q9H074-2; P10242: MYB; NbExp=3; IntAct=EBI-12101100, EBI-298355;
CC Q9H074-2; PRO_0000338257 [P0C6U8]: 1a; Xeno; NbExp=7; IntAct=EBI-12101100, EBI-25635190;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H074-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H074-2; Sequence=VSP_010005;
CC Name=3;
CC IsoId=Q9H074-3; Sequence=VSP_047503;
CC -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates
CC translation initiation.
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; AF013758; AAC39697.2; -; mRNA.
DR EMBL; AL136920; CAB66854.1; -; mRNA.
DR EMBL; AC114956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005295; AAH05295.1; -; mRNA.
DR EMBL; BC015937; AAH15937.1; -; mRNA.
DR EMBL; DB089732; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS3947.1; -. [Q9H074-1]
DR CCDS; CCDS3948.1; -. [Q9H074-3]
DR CCDS; CCDS47204.1; -. [Q9H074-2]
DR RefSeq; NP_006442.2; NM_006451.4. [Q9H074-1]
DR RefSeq; NP_877590.1; NM_182789.3. [Q9H074-2]
DR RefSeq; NP_899152.1; NM_183323.2. [Q9H074-3]
DR RefSeq; XP_005248287.1; XM_005248230.3. [Q9H074-3]
DR RefSeq; XP_016864445.1; XM_017008956.1. [Q9H074-3]
DR PDB; 1JH4; NMR; -; B=123-144.
DR PDB; 3NTW; X-ray; 2.60 A; B/D=123-144.
DR PDB; 3RK6; X-ray; 2.00 A; A/B=157-373.
DR PDB; 6YXJ; X-ray; 3.50 A; B=157-375.
DR PDBsum; 1JH4; -.
DR PDBsum; 3NTW; -.
DR PDBsum; 3RK6; -.
DR PDBsum; 6YXJ; -.
DR AlphaFoldDB; Q9H074; -.
DR BMRB; Q9H074; -.
DR SMR; Q9H074; -.
DR BioGRID; 115851; 131.
DR ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
DR CORUM; Q9H074; -.
DR ELM; Q9H074; -.
DR IntAct; Q9H074; 37.
DR MINT; Q9H074; -.
DR STRING; 9606.ENSP00000302768; -.
DR GlyGen; Q9H074; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H074; -.
DR MetOSite; Q9H074; -.
DR PhosphoSitePlus; Q9H074; -.
DR SwissPalm; Q9H074; -.
DR BioMuta; PAIP1; -.
DR DMDM; 46397025; -.
DR EPD; Q9H074; -.
DR jPOST; Q9H074; -.
DR MassIVE; Q9H074; -.
DR MaxQB; Q9H074; -.
DR PaxDb; Q9H074; -.
DR PeptideAtlas; Q9H074; -.
DR PRIDE; Q9H074; -.
DR ProteomicsDB; 1433; -.
DR ProteomicsDB; 80210; -. [Q9H074-1]
DR ProteomicsDB; 80211; -. [Q9H074-2]
DR Antibodypedia; 10789; 202 antibodies from 27 providers.
DR DNASU; 10605; -.
DR Ensembl; ENST00000306846.8; ENSP00000302768.3; ENSG00000172239.14. [Q9H074-1]
DR Ensembl; ENST00000338972.8; ENSP00000339622.4; ENSG00000172239.14. [Q9H074-3]
DR Ensembl; ENST00000436644.6; ENSP00000387729.2; ENSG00000172239.14. [Q9H074-2]
DR GeneID; 10605; -.
DR KEGG; hsa:10605; -.
DR MANE-Select; ENST00000306846.8; ENSP00000302768.3; NM_006451.5; NP_006442.2.
DR UCSC; uc003joa.4; human. [Q9H074-1]
DR CTD; 10605; -.
DR DisGeNET; 10605; -.
DR GeneCards; PAIP1; -.
DR HGNC; HGNC:16945; PAIP1.
DR HPA; ENSG00000172239; Low tissue specificity.
DR MIM; 605184; gene.
DR neXtProt; NX_Q9H074; -.
DR OpenTargets; ENSG00000172239; -.
DR PharmGKB; PA134941557; -.
DR VEuPathDB; HostDB:ENSG00000172239; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000153432; -.
DR HOGENOM; CLU_044856_1_0_1; -.
DR InParanoid; Q9H074; -.
DR OMA; EFVPFGM; -.
DR OrthoDB; 1384163at2759; -.
DR PhylomeDB; Q9H074; -.
DR TreeFam; TF325625; -.
DR PathwayCommons; Q9H074; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR SignaLink; Q9H074; -.
DR BioGRID-ORCS; 10605; 31 hits in 1078 CRISPR screens.
DR ChiTaRS; PAIP1; human.
DR EvolutionaryTrace; Q9H074; -.
DR GeneWiki; PAIP1; -.
DR GenomeRNAi; 10605; -.
DR Pharos; Q9H074; Tbio.
DR PRO; PR:Q9H074; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H074; protein.
DR Bgee; ENSG00000172239; Expressed in cortical plate and 102 other tissues.
DR ExpressionAtlas; Q9H074; baseline and differential.
DR Genevisible; Q9H074; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; TAS:ProtInc.
DR IDEAL; IID00586; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF07145; PAM2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Host-virus interaction; Methylation; Reference proteome;
KW Translation regulation.
FT CHAIN 1..479
FT /note="Polyadenylate-binding protein-interacting protein 1"
FT /id="PRO_0000058177"
FT DOMAIN 159..376
FT /note="MIF4G"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..143
FT /note="PABPC1-interacting motif-2 (PAM2)"
FT REGION 157..375
FT /note="PAIP1 middle domain (PAIP1M)"
FT /evidence="ECO:0000303|PubMed:33876849"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..479
FT /note="PABPC1-interacting motif-1 (PAM1)"
FT COMPBIAS 49..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047503"
FT VAR_SEQ 10..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010005"
FT CONFLICT 239
FT /note="R -> C (in Ref. 4; AAH15937)"
FT /evidence="ECO:0000305"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:3RK6"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 313..336
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:3RK6"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:3RK6"
FT INIT_MET Q9H074-3:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q9H074-3:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 479 AA; 53525 MW; A4820607190A3A43 CRC64;
MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA PGFLQPPPLR
QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS QDKIPQQNSE SAMAKPQVVV
APVLMSKLSV NAPEFYPSGY SSSYTESYED GCEDYPTLSE YVQDFLNHLT EQPGSFETEI
EQFAETLNGC VTTDDALQEL VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ
LLLQRCRTEY EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL
RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE NVVLDANCSR
DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN EPTFYTSDGV PFTAADPDYQ
EKYQELLERE DFFPDYEENG TDLSGAGDPY LDDIDDEMDP EIEEAYEKFC LESERKRKQ
