FEM1B_MOUSE
ID FEM1B_MOUSE Reviewed; 627 AA.
AC Q9Z2G0; Q3TV57; Q3ULQ3; Q3V148; Q80U13; Q99NC9; Q9QZL3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein fem-1 homolog B {ECO:0000305};
DE Short=FEM1b {ECO:0000303|PubMed:9828124};
DE AltName: Full=FEM1-beta;
DE AltName: Full=Fem-1-like death receptor-binding protein alpha {ECO:0000303|PubMed:10542291};
DE AltName: Full=Fem-1-like in apoptotic pathway protein alpha {ECO:0000303|PubMed:10542291};
DE Short=F1A-alpha {ECO:0000303|PubMed:10542291};
DE AltName: Full=mt-Fem {ECO:0000303|Ref.3};
GN Name=Fem1b {ECO:0000303|PubMed:9828124, ECO:0000312|MGI:MGI:1335087};
GN Synonyms=F1aa {ECO:0000303|PubMed:10542291}, Kiaa0396;
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], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=9828124; DOI=10.1006/geno.1998.5569;
RA Ventura-Holman T., Seldin M.F., Li W., Maher J.F.;
RT "The murine fem1 gene family: homologs of the Caenorhabditis elegans sex-
RT determination protein FEM-1.";
RL Genomics 54:221-230(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10542291; DOI=10.1074/jbc.274.45.32461;
RA Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.;
RT "F1Aalpha, a death receptor-binding protein homologous to the
RT Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase
RT substrate that mediates apoptosis.";
RL J. Biol. Chem. 274:32461-32468(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Tanaka H., Koga M., Nishimune Y.;
RT "Haploid germ cell specific gene.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Olfactory bulb, Retina, Testis, and 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].
RC STRAIN=C57BL/6J; TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-627.
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PHTF1.
RX PubMed=15601915; DOI=10.1095/biolreprod.104.035964;
RA Oyhenart J., Benichou S., Raich N.;
RT "Putative homeodomain transcription factor 1 interacts with the
RT feminization factor homolog fem1b in male germ cells.";
RL Biol. Reprod. 72:780-787(2005).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16024793; DOI=10.1128/mcb.25.15.6570-6577.2005;
RA Lu D., Ventura-Holman T., Li J., McMurray R.W., Subauste J.S., Maher J.F.;
RT "Abnormal glucose homeostasis and pancreatic islet function in mice with
RT inactivation of the Fem1b gene.";
RL Mol. Cell. Biol. 25:6570-6577(2005).
RN [9]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH NKX3-1.
RX PubMed=18816836; DOI=10.1002/dvdy.21694;
RA Wang X., Desai N., Hu Y.P., Price S.M., Abate-Shen C., Shen M.M.;
RT "Mouse Fem1b interacts with the Nkx3.1 homeoprotein and is required for
RT proper male secondary sexual development.";
RL Dev. Dyn. 237:2963-2972(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21723927; DOI=10.1016/j.gene.2011.06.025;
RA Shi Y.Q., Liao S.Y., Zhuang X.J., Han C.S.;
RT "Mouse Fem1b interacts with and induces ubiquitin-mediated degradation of
RT Ankrd37.";
RL Gene 485:153-159(2011).
RN [12]
RP FUNCTION, IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, AND
RP MUTAGENESIS OF CYS-186 AND LEU-597.
RX PubMed=32941802; DOI=10.1016/j.cell.2020.08.034;
RA Manford A.G., Rodriguez-Perez F., Shih K.Y., Shi Z., Berdan C.A., Choe M.,
RA Titov D.V., Nomura D.K., Rape M.;
RT "A cellular mechanism to detect and alleviate reductive stress.";
RL Cell 183:46-61(2020).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation (By similarity). The C-degron recognized by the DesCEND
CC pathway is usually a motif of less than ten residues and can be present
CC in full-length proteins, truncated proteins or proteolytically cleaved
CC forms (By similarity). The CRL2(FEM1B) complex specifically recognizes
CC proteins ending with -Gly-Leu-Asp-Arg, such as CDK5R1, leading to their
CC ubiquitination and degradation (By similarity). Also acts as a
CC regulator of the reductive stress response by mediating ubiquitination
CC of reduced FNIP1: in response to reductive stress, the CRL2(FEM1B)
CC complex specifically recognizes a conserved Cys degron in FNIP1 when
CC this degron is reduced, leading to FNIP1 degradation and subsequent
CC activation of mitochondria to recalibrate reactive oxygen species (ROS)
CC (PubMed:32941802). Promotes ubiquitination of GLI1, suppressing GLI1
CC transcriptional activator activity (By similarity). Promotes
CC ubiquitination and degradation of ANKRD37 (PubMed:21723927). Promotes
CC ubiquitination and degradation of SLBP (By similarity). Involved in
CC apoptosis by acting as a death receptor-associated protein that
CC mediates apoptosis (By similarity). Also involved in glucose
CC homeostasis in pancreatic islet (PubMed:16024793). May also act as an
CC adapter/mediator in replication stress-induced signaling that leads to
CC the activation of CHEK1 (By similarity). {ECO:0000250|UniProtKB:Q9UK73,
CC ECO:0000269|PubMed:16024793, ECO:0000269|PubMed:21723927,
CC ECO:0000269|PubMed:32941802}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UK73}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC FEM1B (PubMed:32941802). Homooligomer (By similarity). Interacts with
CC PPM1F and PHTF1 (PubMed:15601915). Interacts with the death domain of
CC FAS/TNFRSF6 and TNFRSF1A. Interacts with CHEK1 (By similarity).
CC Interacts with NKX3-1 (PubMed:18816836). {ECO:0000250|UniProtKB:Q9UK73,
CC ECO:0000269|PubMed:15601915, ECO:0000269|PubMed:18816836,
CC ECO:0000269|PubMed:32941802}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601915,
CC ECO:0000269|PubMed:21723927}. Nucleus {ECO:0000250|UniProtKB:Q9UK73}.
CC Note=In the nucleus, the protein level increased slightly after
CC camptothecin (CPT) treatment. Associated with chromatin.
CC {ECO:0000250|UniProtKB:Q9UK73}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic islets, within both beta
CC cells and non-beta cells (at protein level) (PubMed:16024793). Highly
CC expressed in adult testis; expressed in all types of spermatogonia
CC (PubMed:9828124, PubMed:18816836). Also expressed in the prostate of
CC neonatal mice (PubMed:18816836). {ECO:0000269|PubMed:16024793,
CC ECO:0000269|PubMed:18816836, ECO:0000269|PubMed:9828124}.
CC -!- DISRUPTION PHENOTYPE: Abnormal glucose tolerance predominantly due to
CC defective glucose-stimulated insulin secretion (PubMed:16024793). Mice
CC also show defects in prostate ductal morphogenesis and secretory
CC protein expression (PubMed:18816836). {ECO:0000269|PubMed:16024793,
CC ECO:0000269|PubMed:18816836}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR EMBL; AF064448; AAC82373.1; -; mRNA.
DR EMBL; AF178633; AAF05315.1; -; mRNA.
DR EMBL; AB022863; BAB33298.1; -; mRNA.
DR EMBL; AK032338; BAC27822.1; -; mRNA.
DR EMBL; AK132692; BAE21305.1; -; mRNA.
DR EMBL; AK145371; BAE26395.1; -; mRNA.
DR EMBL; AK149329; BAE28816.1; -; mRNA.
DR EMBL; AK154060; BAE32347.1; -; mRNA.
DR EMBL; AK160393; BAE35763.1; -; mRNA.
DR EMBL; BC068236; AAH68236.1; -; mRNA.
DR EMBL; AK122272; BAC65554.1; -; mRNA.
DR CCDS; CCDS23266.1; -.
DR RefSeq; NP_034323.1; NM_010193.4.
DR PDB; 7ROY; X-ray; 2.90 A; A/B/C/D=1-377.
DR PDBsum; 7ROY; -.
DR AlphaFoldDB; Q9Z2G0; -.
DR SMR; Q9Z2G0; -.
DR BioGRID; 199631; 3.
DR IntAct; Q9Z2G0; 1.
DR STRING; 10090.ENSMUSP00000034775; -.
DR iPTMnet; Q9Z2G0; -.
DR PhosphoSitePlus; Q9Z2G0; -.
DR EPD; Q9Z2G0; -.
DR MaxQB; Q9Z2G0; -.
DR PaxDb; Q9Z2G0; -.
DR PeptideAtlas; Q9Z2G0; -.
DR PRIDE; Q9Z2G0; -.
DR ProteomicsDB; 267726; -.
DR Antibodypedia; 13914; 239 antibodies from 32 providers.
DR Ensembl; ENSMUST00000034775; ENSMUSP00000034775; ENSMUSG00000032244.
DR GeneID; 14155; -.
DR KEGG; mmu:14155; -.
DR UCSC; uc009qam.3; mouse.
DR CTD; 10116; -.
DR MGI; MGI:1335087; Fem1b.
DR VEuPathDB; HostDB:ENSMUSG00000032244; -.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000161115; -.
DR HOGENOM; CLU_020042_1_0_1; -.
DR InParanoid; Q9Z2G0; -.
DR OMA; NKHIYDL; -.
DR OrthoDB; 252380at2759; -.
DR PhylomeDB; Q9Z2G0; -.
DR TreeFam; TF351376; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 14155; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fem1b; mouse.
DR PRO; PR:Q9Z2G0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z2G0; protein.
DR Bgee; ENSMUSG00000032244; Expressed in primitive streak and 249 other tissues.
DR Genevisible; Q9Z2G0; MM.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005123; F:death receptor binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Apoptosis; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..627
FT /note="Protein fem-1 homolog B"
FT /id="PRO_0000324531"
FT REPEAT 45..74
FT /note="ANK 1"
FT REPEAT 87..116
FT /note="ANK 2"
FT REPEAT 120..149
FT /note="ANK 3"
FT REPEAT 153..182
FT /note="ANK 4"
FT REPEAT 186..215
FT /note="ANK 5"
FT REPEAT 218..248
FT /note="ANK 6"
FT REPEAT 344..377
FT /note="TPR"
FT REPEAT 483..527
FT /note="ANK 7"
FT REPEAT 531..568
FT /note="ANK 8"
FT SITE 342..343
FT /note="Cleavage; by a caspase-3-like protease"
FT /evidence="ECO:0000250|UniProtKB:Q9UK73"
FT MUTAGEN 186
FT /note="C->S: Abolished ability to promote ubiquitination of
FT reduced FNIP1."
FT /evidence="ECO:0000269|PubMed:32941802"
FT MUTAGEN 597
FT /note="L->A: Abolished ability to promote ubiquitination of
FT reduced FNIP1."
FT /evidence="ECO:0000269|PubMed:32941802"
FT CONFLICT 184
FT /note="A -> V (in Ref. 4; BAE21305)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> G (in Ref. 2; AAF05315)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="L -> R (in Ref. 3; BAB33298)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="V -> A (in Ref. 2; AAF05315)"
FT /evidence="ECO:0000305"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:7ROY"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:7ROY"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:7ROY"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:7ROY"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:7ROY"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:7ROY"
SQ SEQUENCE 627 AA; 70223 MW; 72D4ABA2D4576F1B CRC64;
MEGLAGYVYK AASEGKVLTL AALLLNRSES DIRYLLGYVS QQGGQRSTPL IIAARNGHAK
VVRLLLEHYR VQTQQTGTVR FDGYVIDGAT ALWCAAGAGH FEVVKLLVSH GANVNHTTVT
NSTPLRAACF DGRLDIVKYL VENNANISIA NKYDNTCLMI AAYKGHTDVV RYLLEQRADP
NAKAHCGATA LHFAAEAGHI DIVKELIKWR AAIVVNGHGM TPLKVAAESC KADVVELLLS
HADCDRRSRI EALELLGASF ANDRENYDIM KTYHYLYLAM LERFQDGDNI LEKEVLPPIH
AYGNRTECRN PQELEAIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR GAVYADNMEF
EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE AVKAPDIECV LRCSVLEIEQ
SMNRVKNISD ADVHSAMDNY ECNLYTFLYL VCISTKTQCS EEDQCRINKQ IYNLIHLDPR
TREGFSLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
AARAVRANDI NYQDQIPRTL EEFVGFH
