I5P2_MOUSE
ID I5P2_MOUSE Reviewed; 993 AA.
AC Q8K337; O54996; Q8CF65; Q91ZF8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Type II inositol 1,4,5-trisphosphate 5-phosphatase;
DE EC=3.1.3.36;
DE AltName: Full=Inositol polyphosphate-5-phosphatase B;
DE AltName: Full=Phosphoinositide 5-phosphatase;
DE Short=5PTase;
DE Flags: Precursor;
GN Name=Inpp5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11311145; DOI=10.1042/bj3550805;
RA O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W.,
RA Sambrook J., Mitchell C.A.;
RT "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the
RT absence of all three yeast Sac1-like-domain-containing 5-phosphatases.";
RL Biochem. J. 355:805-817(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [MRNA] OF 204-993 (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Kidney;
RX PubMed=9525932; DOI=10.1074/jbc.273.14.8256;
RA Matzaris M., O'Malley C.J., Badger A., Speed C.J., Bird P.I.,
RA Mitchell C.A.;
RT "Distinct membrane and cytosolic forms of inositol polyphosphate 5-
RT phosphatase II. Efficient membrane localization requires two discrete
RT domains.";
RL J. Biol. Chem. 273:8256-8267(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH APPL1.
RX PubMed=22072788; DOI=10.1091/mbc.e11-06-0489;
RA Bohdanowicz M., Balkin D.M., De Camilli P., Grinstein S.;
RT "Recruitment of OCRL and Inpp5B to phagosomes by Rab5 and APPL1 depletes
RT phosphoinositides and attenuates Akt signaling.";
RL Mol. Biol. Cell 23:176-187(2012).
RN [8]
RP INTERACTION WITH INPP5F.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [9]
RP STRUCTURE BY NMR OF 1-156, AND PH DOMAIN.
RX PubMed=19536138; DOI=10.1038/emboj.2009.155;
RA Mao Y., Balkin D.M., Zoncu R., Erdmann K.S., Tomasini L., Hu F., Jin M.M.,
RA Hodsdon M.E., De Camilli P.;
RT "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to
RT phosphoinositide metabolism.";
RL EMBO J. 28:1831-1842(2009).
CC -!- FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate
CC (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-
CC trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular
CC signaling events. {ECO:0000269|PubMed:11311145,
CC ECO:0000269|PubMed:9525932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:9525932};
CC -!- SUBUNIT: Interacts with APPL1, PHETA1 and PHETA2. Interacts with
CC several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A
CC and RAB33B; these interactions may play a dual role in targeting INPP5B
CC to the specific membranes and stimulating its phosphatase activity.
CC Interacts preferentially with non-phosphorylated RAB8A; phosphoryation
CC of RAB8A on 'Thr-72' disrupts this interaction (By similarity).
CC Interacts with INPP5F (PubMed:25869668). {ECO:0000250|UniProtKB:P32019,
CC ECO:0000269|PubMed:25869668}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9525932}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:P32019}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P32019}. Membrane
CC {ECO:0000250|UniProtKB:P32019}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P32019}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P32019}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:9525932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K337-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K337-2; Sequence=VSP_042226, VSP_042227;
CC Name=3;
CC IsoId=Q8K337-3; Sequence=VSP_042224, VSP_042225;
CC -!- TISSUE SPECIFICITY: Detected in kidney, liver, brain, lung and testis
CC (at protein level). Detected in kidney and liver, and at lower levels
CC in brain, lung and testis. {ECO:0000269|PubMed:9525932}.
CC -!- DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating)
CC domains form a single folding module. The ASH domain has an
CC immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic
CC arginine and is catalytically inactive. The ASH-RhoGAP module regulates
CC the majority of the protein-protein interactions currently described.
CC The ASH domain mediates association with membrane-targeting Rab
CC GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1,
CC which is then displaced by PHETA1 and PHETA2 as endosomes mature, all
CC three interactions rely on F&H motifs, an approximately 12-13 amino-
CC acid sequence centered around Phe and His residues essential for
CC binding (By similarity). {ECO:0000250}.
CC -!- PTM: Isoprenylation at Cys-990 may be required for localization at the
CC membrane. {ECO:0000250}.
CC -!- PTM: May be proteolytically cleaved after Lys-320 as inferred from N-
CC terminal protein sequence of the 75 kda form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB95412.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY007563; AAG23293.1; -; mRNA.
DR EMBL; AK004601; BAC25089.1; -; mRNA.
DR EMBL; AL606907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028864; AAH28864.1; -; mRNA.
DR EMBL; AF040094; AAB95412.2; ALT_INIT; mRNA.
DR CCDS; CCDS38876.1; -. [Q8K337-1]
DR PIR; T42384; T42384.
DR RefSeq; NP_032411.3; NM_008385.4. [Q8K337-1]
DR PDB; 2KIG; NMR; -; A=1-156.
DR PDBsum; 2KIG; -.
DR AlphaFoldDB; Q8K337; -.
DR SMR; Q8K337; -.
DR BioGRID; 200768; 37.
DR IntAct; Q8K337; 29.
DR STRING; 10090.ENSMUSP00000092375; -.
DR iPTMnet; Q8K337; -.
DR PhosphoSitePlus; Q8K337; -.
DR EPD; Q8K337; -.
DR MaxQB; Q8K337; -.
DR PaxDb; Q8K337; -.
DR PeptideAtlas; Q8K337; -.
DR PRIDE; Q8K337; -.
DR ProteomicsDB; 266941; -. [Q8K337-1]
DR ProteomicsDB; 266942; -. [Q8K337-2]
DR ProteomicsDB; 266943; -. [Q8K337-3]
DR ABCD; Q8K337; 1 sequenced antibody.
DR Antibodypedia; 31808; 172 antibodies from 25 providers.
DR DNASU; 16330; -.
DR Ensembl; ENSMUST00000094782; ENSMUSP00000092375; ENSMUSG00000028894. [Q8K337-1]
DR Ensembl; ENSMUST00000184454; ENSMUSP00000139221; ENSMUSG00000028894. [Q8K337-2]
DR GeneID; 16330; -.
DR KEGG; mmu:16330; -.
DR UCSC; uc008uqy.2; mouse. [Q8K337-1]
DR UCSC; uc008uqz.1; mouse. [Q8K337-3]
DR CTD; 3633; -.
DR MGI; MGI:103257; Inpp5b.
DR VEuPathDB; HostDB:ENSMUSG00000028894; -.
DR eggNOG; KOG0565; Eukaryota.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000156762; -.
DR HOGENOM; CLU_006779_2_0_1; -.
DR InParanoid; Q8K337; -.
DR OMA; ECANNYL; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; Q8K337; -.
DR TreeFam; TF317034; -.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR BioGRID-ORCS; 16330; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Inpp5b; mouse.
DR EvolutionaryTrace; Q8K337; -.
DR PRO; PR:Q8K337; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K337; protein.
DR Bgee; ENSMUSG00000028894; Expressed in right lung lobe and 250 other tissues.
DR ExpressionAtlas; Q8K337; baseline and differential.
DR Genevisible; Q8K337; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0070613; P:regulation of protein processing; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd09093; INPP5c_INPP5B; 1.
DR CDD; cd13383; PH_OCRL2; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR031896; INPP5B_PH_dom.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF16776; INPP5B_PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Hydrolase; Lipid metabolism; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Methylation; Prenylation; Reference proteome.
FT CHAIN 1..990
FT /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase"
FT /id="PRO_0000415365"
FT PROPEP 991..993
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422294"
FT DOMAIN 22..148
FT /note="PH"
FT DOMAIN 821..993
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 149..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..668
FT /note="5-phosphatase"
FT /evidence="ECO:0000250"
FT REGION 669..782
FT /note="ASH"
FT /evidence="ECO:0000250"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 459..460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 582..583
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 596..598
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 990
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 990
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..251
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042224"
FT VAR_SEQ 252..258
FT /note="RERDCAG -> MKGKLLC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042225"
FT VAR_SEQ 811..825
FT /note="LMSVQTADDRSQLEN -> PGCQCNGAAAVLARG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11311145"
FT /id="VSP_042226"
FT VAR_SEQ 826..993
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11311145"
FT /id="VSP_042227"
FT CONFLICT 993
FT /note="L -> P (in Ref. 2; BAC25089)"
FT /evidence="ECO:0000305"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 30..43
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:2KIG"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:2KIG"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2KIG"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2KIG"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:2KIG"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2KIG"
SQ SEQUENCE 993 AA; 112762 MW; C15670755B562878 CRC64;
MDQSVAIQET LVEGEYCVIA VQGVLCKGDS RQSRLLGLVR YRLENDAQEH ALFLYTHRRM
AITGDDVSLD QIVPLSKDFM LEEVSPDGEL YILGSDVTVQ LNTAELKLVF QLPFGSHTRT
FLQEVARACP GFDPETRDPE FEWLSRHTCA EPDAESPKPR EWNSDPGTRS GFAPIGGSRH
QSRNARRGLE DVLPRGPGYI LLWGGAAEEP EFLLAEEMHE GGPVRGRRPL AGRRDEALEE
ADWEMSAGGG SRERDCAGVS NVDSSRPNGR GPDQPSGARC PEKPENSLTR QNKSKSDMSE
KVRSATVTVS DKAHILSVQK FGLRDTIVRS HLVQKEENYT YIQNFRFFVG TYNVNGQSPK
ECLRPWLSHS ALAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSESL HPDAKYAKVK
FVRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQLH NTSICVVNSH
LAAHTEEYER RNQDYRDICS RMQFPQVDPS QPPLTINKHD VILWLGDLNY RIEELDVGKV
KKLVEEKAFQ TLYAHDQLKI QVAARTIFDG FTEGEITFQP TYKYDTGSDD WDTSEKCRAP
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNEELYRK TLEEIVRSLD
KMENANIPSV TLSKREFCFE NVKYMQLQTE SFTIHNSQVP CQFEFINKPD EESYCKQWLT
ARPSKGFLLP DSHVEIELEL FVNKSTATKL NSGKDTIEDI LVLHLERGKD YFLSVSGNYL
PSCFGSPIHT LCYMREPILD LPLKTVSDLT LMSVQTADDR SQLENPMEIP KELWMMVDYL
YRNAVQQEDL FQQPGLRPEF DHIRDCLDTG MIDQLCANNH SVAEALLLFL ESLPEPVICY
SAYHSCLECS GNYAASKQII LTLPSFHKNV FNYLMAFLQE LLKNSANNHL DENILASIFG
SLLLRNPARH QKLDMAEKKK AQEFIHQFLC GPL
