ID   FKBP4_MOUSE             Reviewed;         458 AA.
AC   P30416; Q3TVC9;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   17-JUN-2020, entry version 195.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP4;
DE            Short=PPIase FKBP4;
DE            EC=5.2.1.8;
DE   AltName: Full=52 kDa FK506-binding protein;
DE            Short=52 kDa FKBP;
DE            Short=FKBP-52;
DE   AltName: Full=59 kDa immunophilin;
DE            Short=p59;
DE   AltName: Full=FK506-binding protein 4;
DE            Short=FKBP-4;
DE   AltName: Full=FKBP59;
DE   AltName: Full=HSP-binding immunophilin;
DE            Short=HBI;
DE   AltName: Full=Immunophilin FKBP52;
DE   AltName: Full=Rotamase;
DE   Contains:
DE     RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed;
GN   Name=Fkbp4; Synonyms=Fkpb52;
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].
RX   PubMed=7693550; DOI=10.1016/0378-1119(93)90206-i;
RA   Schmitt J., Stunnenberg H.G.;
RT   "Cloning and expression of a mouse cDNA encoding p59, an immunophilin that
RT   associates with the glucocorticoid receptor.";
RL   Gene 132:267-271(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal ganglion;
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 MRNA].
RC   TISSUE=Lung 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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-458, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=8341706; DOI=10.1073/pnas.90.14.6839;
RA   Alnemri E.S., Fernandes-Alnemri T., Nelki D.S., Dudley K., Dubois G.C.,
RA   Litwack G.;
RT   "Overexpression, characterization, and purification of a recombinant mouse
RT   immunophilin FKBP-52 and identification of an associated phosphoprotein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6839-6843(1993).
RN   [5]
RP   IDENTIFICATION IN A COMPLEX WITH NR3C1 AND HSP90AA1.
RX   PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
RA   Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
RA   Chinkers M., Pratt W.B.;
RT   "Protein phosphatase 5 is a major component of glucocorticoid
RT   receptor.hsp90 complexes with properties of an FK506-binding
RT   immunophilin.";
RL   J. Biol. Chem. 272:16224-16230(1997).
RN   [6]
RP   FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX WITH
RP   HSP90AA1 AND NR3C1, AND INTERACTION WITH DYNEIN.
RX   PubMed=11278753; DOI=10.1074/jbc.m010809200;
RA   Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.;
RT   "Evidence that the peptidylprolyl isomerase domain of the hsp90-binding
RT   immunophilin FKBP52 is involved in both dynein interaction and
RT   glucocorticoid receptor movement to the nucleus.";
RL   J. Biol. Chem. 276:14884-14889(2001).
RN   [7]
RP   FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX WITH
RP   HSP90AA1 AND NR3C1, SUBCELLULAR LOCATION, AND INTERACTION WITH DYNEIN.
RX   PubMed=11751894; DOI=10.1074/jbc.c100531200;
RA   Davies T.H., Ning Y.M., Sanchez E.R.;
RT   "A new first step in activation of steroid receptors: hormone-induced
RT   switching of FKBP51 and FKBP52 immunophilins.";
RL   J. Biol. Chem. 277:4597-4600(2002).
RN   [8]
RP   PROTEIN SEQUENCE OF 235-244.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-373, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Immunophilin protein with PPIase and co-chaperone activities.
CC       Component of steroid receptors heterocomplexes through interaction with
CC       heat-shock protein 90 (HSP90). May play a role in the intracellular
CC       trafficking of heterooligomeric forms of steroid hormone receptors
CC       between cytoplasm and nuclear compartments. The isomerase activity
CC       controls neuronal growth cones via regulation of TRPC1 channel opening.
CC       Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU
CC       ability to promote microtubule assembly. May have a protective role
CC       against oxidative stress in mitochondria. {ECO:0000269|PubMed:11278753,
CC       ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- ACTIVITY REGULATION: Inhibited by FK506. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with GLMN (By
CC       similarity). Associates with HSP90AA1 and HSPA1A/HSPA1B in steroid
CC       hormone receptor complexes. Also interacts with peroxisomal phytanoyl-
CC       CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein.
CC       Interacts with HSF1 in the HSP90 complex. Associates with tubulin.
CC       Interacts with MAPT/TAU (By similarity). Interacts (via TPR domain)
CC       with S100A1, S100A2 and S100A6; the interaction is Ca(2+) dependent.
CC       Interaction with S100A1 and S100A2 (but not with S100A6) leads to
CC       inhibition of FKBP4-HSP90 interaction. Interacts with dynein;
CC       contributes to NR3C1 transport to the nucleus. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q02790, ECO:0000250|UniProtKB:Q9QVC8,
CC       ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:11751894,
CC       ECO:0000269|PubMed:9195923}.
CC   -!- INTERACTION:
CC       P30416; P06537: Nr3c1; NbExp=3; IntAct=EBI-492746, EBI-492753;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11751894}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q02790}. Nucleus
CC       {ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Note=Shuttles from mitochondria to nucleus;
CC       co-localizes in mitochondria with the glucocorticoid receptor.
CC       Colocalized with MAPT/TAU in the distal part of the primary cortical
CC       neurons. {ECO:0000250|UniProtKB:Q02790, ECO:0000250|UniProtKB:Q9QVC8}.
CC   -!- DOMAIN: The PPIase activity is mainly due to the first PPIase FKBP-type
CC       domain (1-138 AA). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal region (AA 375-458) is required to prevent
CC       tubulin polymerization. {ECO:0000250}.
CC   -!- DOMAIN: The chaperone activity resides in the C-terminal region, mainly
CC       between amino acids 264 and 400. {ECO:0000250}.
CC   -!- DOMAIN: The TPR repeats mediate mitochondrial localization.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation by CK2 results in loss of HSP90 binding activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34914.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA34914.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X70887; CAA50231.1; -; mRNA.
DR   EMBL; AK083912; BAC39057.1; -; mRNA.
DR   EMBL; AK160202; BAE35690.1; -; mRNA.
DR   EMBL; BC003447; AAH03447.1; -; mRNA.
DR   EMBL; X17069; CAC39452.1; -; mRNA.
DR   EMBL; X17068; CAA34914.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS20573.1; -.
DR   PIR; JN0873; JN0873.
DR   RefSeq; NP_034349.1; NM_010219.3.
DR   SMR; P30416; -.
DR   BioGRID; 199685; 5.
DR   IntAct; P30416; 4.
DR   MINT; P30416; -.
DR   STRING; 10090.ENSMUSP00000032508; -.
DR   iPTMnet; P30416; -.
DR   PhosphoSitePlus; P30416; -.
DR   SwissPalm; P30416; -.
DR   REPRODUCTION-2DPAGE; P30416; -.
DR   EPD; P30416; -.
DR   jPOST; P30416; -.
DR   MaxQB; P30416; -.
DR   PaxDb; P30416; -.
DR   PeptideAtlas; P30416; -.
DR   PRIDE; P30416; -.
DR   Antibodypedia; 1205; 606 antibodies.
DR   Ensembl; ENSMUST00000032508; ENSMUSP00000032508; ENSMUSG00000030357.
DR   GeneID; 14228; -.
DR   KEGG; mmu:14228; -.
DR   UCSC; uc009edr.1; mouse.
DR   CTD; 2288; -.
DR   MGI; MGI:95543; Fkbp4.
DR   eggNOG; KOG0543; Eukaryota.
DR   eggNOG; COG0545; LUCA.
DR   GeneTree; ENSGT00940000157200; -.
DR   InParanoid; P30416; -.
DR   KO; K09571; -.
DR   OMA; ELEMLGW; -.
DR   OrthoDB; 897391at2759; -.
DR   PhylomeDB; P30416; -.
DR   TreeFam; TF354214; -.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   Reactome; R-MMU-3371568; Attenuation phase.
DR   Reactome; R-MMU-8939211; ESR-mediated signaling.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 14228; 0 hits in 12 CRISPR screens.
DR   ChiTaRS; Fkbp4; mouse.
DR   PRO; PR:P30416; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P30416; protein.
DR   Bgee; ENSMUSG00000030357; Expressed in mandibular prominence and 300 other tissues.
DR   ExpressionAtlas; P30416; baseline and differential.
DR   Genevisible; P30416; MM.
DR   GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0032767; F:copper-dependent protein binding; ISO:MGI.
DR   GO; GO:0005528; F:FK506 binding; IEA:InterPro.
DR   GO; GO:0035259; F:glucocorticoid receptor binding; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; IDA:MGI.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR   GO; GO:0051219; F:phosphoprotein binding; IDA:MGI.
DR   GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR   GO; GO:0006825; P:copper ion transport; ISO:MGI.
DR   GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR   GO; GO:0046661; P:male sex differentiation; IMP:MGI.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR   GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0030850; P:prostate gland development; IMP:MGI.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   GO; GO:0031503; P:protein-containing complex localization; IDA:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0006463; P:steroid hormone receptor complex assembly; IDA:MGI.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR031212; FKBP4.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR10516; PTHR10516; 1.
DR   PANTHER; PTHR10516:SF25; PTHR10516:SF25; 1.
DR   Pfam; PF00254; FKBP_C; 2.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 2.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Isomerase; Isopeptide bond; Methylation; Microtubule; Mitochondrion;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Rotamase; TPR repeat;
KW   Ubl conjugation.
FT   CHAIN           1..458
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP4"
FT                   /id="PRO_0000391469"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   CHAIN           2..458
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP4, N-
FT                   terminally processed"
FT                   /id="PRO_0000075319"
FT   DOMAIN          50..138
FT                   /note="PPIase FKBP-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   DOMAIN          167..253
FT                   /note="PPIase FKBP-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REPEAT          270..303
FT                   /note="TPR 1"
FT   REPEAT          319..352
FT                   /note="TPR 2"
FT   REPEAT          353..386
FT                   /note="TPR 3"
FT   REGION          267..400
FT                   /note="Interaction with tubulin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in peptidyl-prolyl cis-trans
FT                   isomerase FKBP4; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine; in peptidyl-prolyl cis-trans
FT                   isomerase FKBP4, N-terminally processed; partial"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   MOD_RES         143
FT                   /note="Phosphothreonine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P27124"
FT   MOD_RES         220
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   MOD_RES         282
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   MOD_RES         373
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   CROSSLNK        441
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q02790"
FT   CONFLICT        6..7
FT                   /note="MK -> HE (in Ref. 4; CAC39452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156..163
FT                   /note="TRGEGYAR -> LGVKAMQG (in Ref. 4; CAC39452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203..240
FT                   /note="GLEEAIQRMEKGEHSIVYLKPSYAFGSVGKERFQIPPH -> AWRRPFSAWR
FT                   KESIPSCTSNLAMLLAVWGRRGSRSHRT (in Ref. 4; CAC39452/
FT                   CAA34914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265..272
FT                   /note="EKLEQSNI -> RSWSRATY (in Ref. 4; CAC39452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="H -> R (in Ref. 3; AAH03447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="G -> R (in Ref. 2; BAE35690)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  51572 MW;  CFB2ED49E9B6BA7A CRC64;
     MTAEEMKAAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETPMIG DRVFVHYTGW
     LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG EVCHITCKPE YAYGAAGSPP
     KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIRTRGEG YARPNDGAMV EVALEGYHKD
     RLFDQRELCF EVGEGESLDL PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH
     AELRYEVRLK SFEKAKESWE MSSAEKLEQS NIVKERGTAY FKEGKYKQAL LQYKKIVSWL
     EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG
     EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT RRQLAREKKL YANMFERLAE
     EEHKVKAEVA AGDHPTDAEM KGERNNVAEN QSRVETEA
//