PRAF3_HUMAN
ID PRAF3_HUMAN Reviewed; 188 AA.
AC O75915; B2R6V5; Q53ES3; Q5KU08;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=PRA1 family protein 3;
DE AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 5;
DE Short=ARL-6-interacting protein 5;
DE Short=Aip-5;
DE AltName: Full=Cytoskeleton-related vitamin A-responsive protein;
DE AltName: Full=Dermal papilla-derived protein 11;
DE AltName: Full=GTRAP3-18;
DE AltName: Full=Glutamate transporter EAAC1-interacting protein;
DE AltName: Full=JM5;
DE AltName: Full=Prenylated Rab acceptor protein 2;
DE AltName: Full=Protein JWa;
DE AltName: Full=Putative MAPK-activating protein PM27;
GN Name=ARL6IP5; Synonyms=DERP11, JWA, PRA2, PRAF3; ORFNames=HSPC127;
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].
RX PubMed=12438930; DOI=10.1097/00001756-200211150-00018;
RA Ikemoto M.J., Inoue K., Akiduki S., Osugi T., Imamura T., Ishida N.,
RA Ohtomi M.;
RT "Identification of addicsin/GTRAP3-18 as a chronic morphine-augumented gene
RT in amygdala.";
RL NeuroReport 13:2079-2084(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=15757671; DOI=10.1016/j.febslet.2005.02.037;
RA Schweneker M., Bachmann A.S., Moelling K.;
RT "JM4 is a four-transmembrane protein binding to the CCR5 receptor.";
RL FEBS Lett. 579:1751-1758(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou J.W., Di Y.P., Wu R.;
RT "A novel differentially displayed vitamin A responsive gene that is
RT cytoskeleton related.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X.N., Yu L., Jin L., Hu P.R., Chen S.Y., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to human mRNA for JM4 protein.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Jiang C., Huang C., Wu T., Peng Y., Gu Y., Zhang L., Zhang C., Li Y.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Brain;
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 [13]
RP PROTEIN SEQUENCE OF 1-9, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 1-27; 152-158 AND 160-185, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [15]
RP INDUCTION.
RX PubMed=14761432;
RA Mao W.G., Li A.P., Ye J., Huang S., Li A.Q., Zhou J.W.;
RT "Effect of differentiation inducer and heat stress on the expression of JWA
RT protein and Hsp70 of K562 cells.";
RL Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi 21:253-256(2003).
RN [16]
RP NOMENCLATURE.
RX PubMed=16481131; DOI=10.1016/j.gene.2005.12.009;
RA Fo C.S., Coleman C.S., Wallick C.J., Vine A.L., Bachmann A.S.;
RT "Genomic organization, expression profile, and characterization of the new
RT protein PRA1 domain family, member 2 (PRAF2).";
RL Gene 371:154-165(2006).
RN [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [20]
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).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Regulates intracellular concentrations of taurine and
CC glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport
CC activity by decreasing its affinity for glutamate in a PKC activity-
CC dependent manner. Plays a role in the retention of SLC1A1/EAAC1 in the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8R5J9,
CC ECO:0000250|UniProtKB:Q9ES40}.
CC -!- SUBUNIT: Homodimer. Heterodimer with ARL6IP1. Forms multimers.
CC Interacts with ARL6. Interacts with prenylated RAB1A and RAB3A.
CC Interacts with SLC1A1/EAAC1. Interacts with RTN2 (via first
CC transmembrane domain). Does not interact with VAMP1, VAMP2 or VAMP3.
CC {ECO:0000250|UniProtKB:Q8R5J9, ECO:0000250|UniProtKB:Q9ES40}.
CC -!- INTERACTION:
CC O75915; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-2860752, EBI-740987;
CC O75915; Q96GF1: RNF185; NbExp=3; IntAct=EBI-2860752, EBI-2340249;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ES40}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9ES40}. Note=Also exists as a soluble form in
CC the cytoplasm. Associated with microtubules.
CC {ECO:0000250|UniProtKB:Q9ES40}.
CC -!- INDUCTION: By methyl-beta-cyclodextrin (By similarity). Up-regulated
CC upon induced differentiation and in heat stress. {ECO:0000250,
CC ECO:0000269|PubMed:14761432}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB052638; BAD83603.1; -; mRNA.
DR EMBL; AY102608; AAM28950.1; -; mRNA.
DR EMBL; AB014765; BAC66462.1; -; mRNA.
DR EMBL; AF070523; AAC64360.1; -; mRNA.
DR EMBL; AF115965; AAP97237.1; -; mRNA.
DR EMBL; AF125530; AAF17224.1; -; mRNA.
DR EMBL; AF161476; AAF29091.1; -; mRNA.
DR EMBL; AB097051; BAC77404.1; -; mRNA.
DR EMBL; AK223566; BAD97286.1; ALT_INIT; mRNA.
DR EMBL; AK312731; BAG35602.1; -; mRNA.
DR EMBL; CH471055; EAW65473.1; -; Genomic_DNA.
DR EMBL; BC005143; AAH05143.1; -; mRNA.
DR EMBL; BC020797; AAH20797.1; -; mRNA.
DR CCDS; CCDS2912.1; -.
DR RefSeq; NP_006398.1; NM_006407.3.
DR AlphaFoldDB; O75915; -.
DR BioGRID; 115801; 174.
DR IntAct; O75915; 56.
DR MINT; O75915; -.
DR STRING; 9606.ENSP00000273258; -.
DR TCDB; 9.A.49.1.3; the prenylated rab acceptor protein 1 (pra1) family.
DR GlyGen; O75915; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75915; -.
DR MetOSite; O75915; -.
DR PhosphoSitePlus; O75915; -.
DR SwissPalm; O75915; -.
DR BioMuta; ARL6IP5; -.
DR CPTAC; CPTAC-1632; -.
DR EPD; O75915; -.
DR jPOST; O75915; -.
DR MassIVE; O75915; -.
DR MaxQB; O75915; -.
DR PaxDb; O75915; -.
DR PeptideAtlas; O75915; -.
DR PRIDE; O75915; -.
DR ProteomicsDB; 50270; -.
DR TopDownProteomics; O75915; -.
DR Antibodypedia; 3088; 227 antibodies from 30 providers.
DR DNASU; 10550; -.
DR Ensembl; ENST00000273258.4; ENSP00000273258.3; ENSG00000144746.7.
DR GeneID; 10550; -.
DR KEGG; hsa:10550; -.
DR MANE-Select; ENST00000273258.4; ENSP00000273258.3; NM_006407.4; NP_006398.1.
DR UCSC; uc003dnr.4; human.
DR CTD; 10550; -.
DR DisGeNET; 10550; -.
DR GeneCards; ARL6IP5; -.
DR HGNC; HGNC:16937; ARL6IP5.
DR HPA; ENSG00000144746; Low tissue specificity.
DR MIM; 605709; gene.
DR neXtProt; NX_O75915; -.
DR OpenTargets; ENSG00000144746; -.
DR PharmGKB; PA134898937; -.
DR VEuPathDB; HostDB:ENSG00000144746; -.
DR eggNOG; KOG4050; Eukaryota.
DR GeneTree; ENSGT00390000008631; -.
DR HOGENOM; CLU_097683_0_0_1; -.
DR InParanoid; O75915; -.
DR OMA; QMKKRYP; -.
DR OrthoDB; 1288023at2759; -.
DR PhylomeDB; O75915; -.
DR TreeFam; TF105479; -.
DR PathwayCommons; O75915; -.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR SignaLink; O75915; -.
DR BioGRID-ORCS; 10550; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; ARL6IP5; human.
DR GeneWiki; ARL6IP5; -.
DR GenomeRNAi; 10550; -.
DR Pharos; O75915; Tbio.
DR PRO; PR:O75915; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75915; protein.
DR Bgee; ENSG00000144746; Expressed in endothelial cell and 216 other tissues.
DR ExpressionAtlas; O75915; baseline and differential.
DR Genevisible; O75915; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0002037; P:negative regulation of L-glutamate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR GO; GO:0051051; P:negative regulation of transport; IBA:GO_Central.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IDA:MGI.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR PANTHER; PTHR12859; PTHR12859; 1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..188
FT /note="PRA1 family protein 3"
FT /id="PRO_0000220883"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 103..117
FT /note="Required for homodimer formation and heterodimer
FT formation with ARL6IP1"
FT /evidence="ECO:0000250|UniProtKB:Q8R5J9"
FT REGION 136..188
FT /note="Targeting to endoplasmic reticulum membrane"
FT /evidence="ECO:0000250|UniProtKB:Q9ES40"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.14,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CONFLICT 28
FT /note="D -> G (in Ref. 10; BAD97286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21615 MW; 3AA708C6D0901B44 CRC64;
MDVNIAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISIVGF
LSPFNMILGG IVVVLVFTGF VWAAHNKDVL RRMKKRYPTT FVMVVMLASY FLISMFGGVM
VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKRT PMGIVLDALE QQEEGINRLT
DYISKVKE
