RASF5_MOUSE
ID RASF5_MOUSE Reviewed; 413 AA.
AC Q5EBH1; O70407; Q6KAR0; Q8C2E8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ras association domain-containing protein 5;
DE AltName: Full=New ras effector 1;
DE AltName: Full=Regulator for cell adhesion and polarization enriched in lymphoid tissues;
DE Short=RAPL;
GN Name=Rassf5; Synonyms=Nore1, Rapl;
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 1), AND INTERACTION WITH HRAS.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9488663; DOI=10.1074/jbc.273.10.5439;
RA Vavvas D., Li X., Avruch J., Zhang X.F.;
RT "Identification of Nore1 as a potential Ras effector.";
RL J. Biol. Chem. 273:5439-5442(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=12845325; DOI=10.1038/ni950;
RA Katagiri K., Maeda A., Shimonaka M., Kinashi T.;
RT "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through
RT spatial regulation of LFA-1.";
RL Nat. Immunol. 4:741-748(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Natural killer cell;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [6]
RP FUNCTION IN APOPTOSIS, AND INTERACTION WITH STK4/MST1; HRAS AND KRAS.
RX PubMed=11864565; DOI=10.1016/s0960-9822(02)00683-8;
RA Khokhlatchev A., Rabizadeh S., Xavier R., Nedwidek M., Chen T., Zhang X.F.,
RA Seed B., Avruch J.;
RT "Identification of a novel Ras-regulated proapoptotic pathway.";
RL Curr. Biol. 12:253-265(2002).
RN [7]
RP SELF-ASSOCIATION, AND INTERACTION WITH RSSF1; HRAS; KRAS; RRAS; RRAS2;
RP MRAS; RAP1B; RAP2A AND RALA.
RX PubMed=11857081; DOI=10.1038/sj.onc.1205192;
RA Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
RA Pfeifer G.P., Avruch J.;
RT "The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes
RT with the Ras-GTP binding protein Nore1.";
RL Oncogene 21:1381-1390(2002).
RN [8]
RP ERRATUM OF PUBMED:11857081.
RA Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
RA Pfeifer G.P., Avruch J.;
RL Oncogene 21:1943-1943(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 [10]
RP STRUCTURE BY NMR OF 95-166, AND SUBUNIT.
RX PubMed=16698549; DOI=10.1016/j.str.2006.03.008;
RA Harjes E., Harjes S., Wohlgemuth S., Mueller K.H., Krieger E., Herrmann C.,
RA Bayer P.;
RT "GTP-Ras disrupts the intramolecular complex of C1 and RA domains of
RT Nore1.";
RL Structure 14:881-888(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 200-357 OF MUTANT ASP-302 IN
RP COMPLEX WITH HRAS, MUTAGENESIS OF CYS-220; LEU-221; PHE-234; LYS-236;
RP ASP-280; LYS-283; GLN-284; LYS-302 AND LYS-303, AND INTERACTION WITH RAP1A.
RX PubMed=18596699; DOI=10.1038/emboj.2008.125;
RA Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A.,
RA Khokhlatchev A., Herrmann C.;
RT "Novel type of Ras effector interaction established between tumour
RT suppressor NORE1A and Ras switch II.";
RL EMBO J. 27:1995-2005(2008).
CC -!- FUNCTION: Potential tumor suppressor. Seems to be involved in
CC lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or
CC chemokine stimulation to integrin activation. Isoform 2 stimulates
CC lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1,
CC resulting in an enhanced adhesion to ICAM1. Together with RAP1A may
CC participate in regulation of microtubule growth. The association of
CC isoform 2 with activated RAP1A is required for directional movement of
CC endothelial cells during wound healing (By similarity). May be involved
CC in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex
CC may mediate HRAS and KRAS induced apoptosis. {ECO:0000250,
CC ECO:0000269|PubMed:11864565}.
CC -!- SUBUNIT: Interacts directly with activated HRAS; a RASSF5-STK4/MST1
CC complex probably associates with activated HRAS (PubMed:9488663,
CC PubMed:11857081, PubMed:11864565, PubMed:18596699). Interacts with KRAS
CC (PubMed:11857081, PubMed:11864565). Probably interacts with Ras-like
CC GTPases RRAS, MRAS, RAP1B, RAP2A and RALA (PubMed:11857081). Interacts
CC with RRAS2 (By similarity). Can self-associate (PubMed:11857081).
CC Interacts with RSSF1 isoform A (PubMed:11857081). The RSSF1 isoform A-
CC RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS
CC (PubMed:11864565, PubMed:11857081). Isoform 2 interacts with activated
CC RAP1A and ITGAL/LFA-1 (By similarity). Binds STK4/MST1, inhibiting
CC STK4/MST1 autoactivation (PubMed:11864565).
CC {ECO:0000250|UniProtKB:Q8WWW0, ECO:0000269|PubMed:11857081,
CC ECO:0000269|PubMed:11864565, ECO:0000269|PubMed:18596699,
CC ECO:0000269|PubMed:9488663}.
CC -!- INTERACTION:
CC Q5EBH1; O88904: Hipk1; NbExp=5; IntAct=EBI-960530, EBI-692945;
CC Q5EBH1; Q61411: Hras; NbExp=2; IntAct=EBI-960530, EBI-400273;
CC Q5EBH1; P23804: Mdm2; NbExp=3; IntAct=EBI-960530, EBI-641788;
CC Q5EBH1; Q9JI11: Stk4; NbExp=3; IntAct=EBI-960530, EBI-1181352;
CC Q5EBH1; P01112: HRAS; Xeno; NbExp=13; IntAct=EBI-960530, EBI-350145;
CC Q5EBH1; P62834: RAP1A; Xeno; NbExp=3; IntAct=EBI-960530, EBI-491414;
CC Q5EBH1-1; P01112: HRAS; Xeno; NbExp=3; IntAct=EBI-960543, EBI-350145;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Isoform 2 is mainly located in the perinuclear
CC region of unstimulated primary T-cells. Upon stimulation translocates
CC to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral
CC zone of the immunological synapse. Isoform 2 is localized to growing
CC microtubules in vascular endothelial cells and is dissociated from
CC microtubules by activated RAP1A (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5EBH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5EBH1-2; Sequence=VSP_019368, VSP_019369;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21397.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF053959; AAC08580.1; -; mRNA.
DR EMBL; AY261333; AAP83361.1; -; mRNA.
DR EMBL; AK131147; BAD21397.1; ALT_INIT; mRNA.
DR EMBL; AK088751; BAC40546.1; -; mRNA.
DR EMBL; AK155534; BAE33312.1; -; mRNA.
DR EMBL; AK155869; BAE33472.1; -; mRNA.
DR EMBL; BC089605; AAH89605.1; -; mRNA.
DR CCDS; CCDS15268.1; -. [Q5EBH1-1]
DR CCDS; CCDS78675.1; -. [Q5EBH1-2]
DR RefSeq; NP_001298023.1; NM_001311094.2. [Q5EBH1-2]
DR RefSeq; NP_061220.2; NM_018750.4. [Q5EBH1-1]
DR PDB; 1RFH; NMR; -; A=108-166.
DR PDB; 2FNF; NMR; -; X=95-166.
DR PDB; 2YMY; X-ray; 1.69 A; A/B=370-413.
DR PDB; 3DDC; X-ray; 1.80 A; B=200-357.
DR PDBsum; 1RFH; -.
DR PDBsum; 2FNF; -.
DR PDBsum; 2YMY; -.
DR PDBsum; 3DDC; -.
DR AlphaFoldDB; Q5EBH1; -.
DR BMRB; Q5EBH1; -.
DR SMR; Q5EBH1; -.
DR BioGRID; 207620; 1.
DR DIP; DIP-29107N; -.
DR IntAct; Q5EBH1; 19.
DR MINT; Q5EBH1; -.
DR STRING; 10090.ENSMUSP00000027688; -.
DR iPTMnet; Q5EBH1; -.
DR PhosphoSitePlus; Q5EBH1; -.
DR SwissPalm; Q5EBH1; -.
DR EPD; Q5EBH1; -.
DR jPOST; Q5EBH1; -.
DR MaxQB; Q5EBH1; -.
DR PaxDb; Q5EBH1; -.
DR PRIDE; Q5EBH1; -.
DR ProteomicsDB; 253172; -. [Q5EBH1-1]
DR ProteomicsDB; 253173; -. [Q5EBH1-2]
DR Antibodypedia; 73646; 282 antibodies from 29 providers.
DR DNASU; 54354; -.
DR Ensembl; ENSMUST00000027688; ENSMUSP00000027688; ENSMUSG00000026430. [Q5EBH1-1]
DR Ensembl; ENSMUST00000068564; ENSMUSP00000067011; ENSMUSG00000026430. [Q5EBH1-2]
DR GeneID; 54354; -.
DR KEGG; mmu:54354; -.
DR UCSC; uc007cnc.1; mouse. [Q5EBH1-2]
DR UCSC; uc007cnd.1; mouse. [Q5EBH1-1]
DR CTD; 83593; -.
DR MGI; MGI:1926375; Rassf5.
DR VEuPathDB; HostDB:ENSMUSG00000026430; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000159288; -.
DR HOGENOM; CLU_045544_1_0_1; -.
DR InParanoid; Q5EBH1; -.
DR OrthoDB; 1120975at2759; -.
DR PhylomeDB; Q5EBH1; -.
DR TreeFam; TF319243; -.
DR BioGRID-ORCS; 54354; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rassf5; mouse.
DR EvolutionaryTrace; Q5EBH1; -.
DR PRO; PR:Q5EBH1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5EBH1; protein.
DR Bgee; ENSMUSG00000026430; Expressed in peripheral lymph node and 234 other tissues.
DR ExpressionAtlas; Q5EBH1; baseline and differential.
DR Genevisible; Q5EBH1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI.
DR GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR033623; RASSF5.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF9; PTHR22738:SF9; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF16517; Nore1-SARAH; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50951; SARAH; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Cytoskeleton;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome;
KW Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..413
FT /note="Ras association domain-containing protein 5"
FT /id="PRO_0000240402"
FT DOMAIN 265..359
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 361..408
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT ZN_FING 117..165
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW0"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW0"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12845325,
FT ECO:0000303|PubMed:15449545, ECO:0000303|PubMed:16141072"
FT /id="VSP_019368"
FT VAR_SEQ 143..188
FT /note="ALRCANCKFTCHSECRSLIQLDCRQKGGPALDRRSPESTLTPTLNQ -> MT
FT VDSSMSSGYCSLDEELEDCFFTAKTTFFRNLQSKQPSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12845325,
FT ECO:0000303|PubMed:15449545, ECO:0000303|PubMed:16141072"
FT /id="VSP_019369"
FT MUTAGEN 220
FT /note="C->A: Reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 220
FT /note="C->D: Strongly reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 221
FT /note="L->A,D: Strongly reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 234
FT /note="F->A: Reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 236
FT /note="K->A: Reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 280
FT /note="D->A: Reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 283
FT /note="K->A: Very strong reduction of the interaction with
FT HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 284
FT /note="Q->A: Reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 302
FT /note="K->D: Reduced specificity for HRAS and diminished
FT discrimination between HRAS and RAP1A."
FT /evidence="ECO:0000269|PubMed:18596699"
FT MUTAGEN 303
FT /note="K->A: Strongly reduced interaction with HRAS."
FT /evidence="ECO:0000269|PubMed:18596699"
FT CONFLICT 179
FT /note="E -> G (in Ref. 1; AAC08580)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..257
FT /note="IRPQSIY -> SGPSPSM (in Ref. 1; AAC08580)"
FT /evidence="ECO:0000305"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2FNF"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1RFH"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1RFH"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1RFH"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1RFH"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3DDC"
FT STRAND 231..245
FT /evidence="ECO:0007829|PDB:3DDC"
FT STRAND 275..288
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3DDC"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:3DDC"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:3DDC"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:3DDC"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3DDC"
FT HELIX 370..405
FT /evidence="ECO:0007829|PDB:2YMY"
SQ SEQUENCE 413 AA; 46714 MW; E6FF7DDE6BECB180 CRC64;
MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALIPAAG ASEDRGGRRS
GRRDPEPTPR DCRHARPVRP GLQPRLRLRP GSHRPRDVRS IFEQPQDPRV LAERGEGHRF
VELALRGGPG WCDLCGREVL RQALRCANCK FTCHSECRSL IQLDCRQKGG PALDRRSPES
TLTPTLNQNV CKAVEETQHP PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK
LRRPVTVPAG IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISST TTVSEVIQGL
LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADYPLYLR LLAGPDTDVL SFVLKENETG
EVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK LEEALRESQG KPG
