MIS_HUMAN
ID MIS_HUMAN Reviewed; 560 AA.
AC P03971; O75246; Q6GTN3;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Muellerian-inhibiting factor;
DE AltName: Full=Anti-Muellerian hormone;
DE Short=AMH;
DE AltName: Full=Muellerian-inhibiting substance {ECO:0000303|PubMed:3754790};
DE Short=MIS {ECO:0000303|PubMed:3754790};
DE Flags: Precursor;
GN Name=AMH {ECO:0000312|HGNC:HGNC:464}; Synonyms=MIF;
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 [GENOMIC DNA], VARIANTS ILE-49 AND ALA-515, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=3754790; DOI=10.1016/0092-8674(86)90783-x;
RA Cate R.L., Mattaliano R.J., Hession C., Tizard R., Farber N.M., Cheung A.,
RA Ninfa E.G., Frey A.Z., Gash D.J., Chow E.P., Fisher R.A., Bertonis J.M.,
RA Torres G., Wallner B.P., Ramachandran K.L., Ragin R.C., Manganaro T.F.,
RA McLaughlin D.T., Donahoe P.K.;
RT "Isolation of the bovine and human genes for Mullerian inhibiting substance
RT and expression of the human gene in animal cells.";
RL Cell 45:685-698(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-515.
RC 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 [4]
RP PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, SUBUNIT, AND PROTEIN SEQUENCE
RP OF 25-34 AND 452-461.
RX PubMed=2974034; DOI=10.1016/s0021-9258(18)37375-7;
RA Pepinsky R.B., Sinclair L.K., Chow E.P., Mattaliano R.J., Manganaro T.F.,
RA Donahoe P.K., Cate R.L.;
RT "Proteolytic processing of mullerian inhibiting substance produces a
RT transforming growth factor-beta-like fragment.";
RL J. Biol. Chem. 263:18961-18964(1988).
RN [5]
RP FUNCTION, SUBUNIT, AND PROTEOLYTIC PROCESSING.
RX PubMed=8469238; DOI=10.1210/mend.7.2.8469238;
RA Wilson C.A., di Clemente N., Ehrenfels C., Pepinsky R.B., Josso N.,
RA Vigier B., Cate R.L.;
RT "Mullerian inhibiting substance requires its N-terminal domain for
RT maintenance of biological activity, a novel finding within the transforming
RT growth factor-beta superfamily.";
RL Mol. Endocrinol. 7:247-257(1993).
RN [6]
RP INDUCTION.
RX PubMed=11779604; DOI=10.1016/s0015-0282(01)02944-2;
RA Cook C.L., Siow Y., Brenner A.G., Fallat M.E.;
RT "Relationship between serum muellerian-inhibiting substance and other
RT reproductive hormones in untreated women with polycystic ovary syndrome and
RT normal women.";
RL Fertil. Steril. 77:141-146(2002).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14742691; DOI=10.1093/molehr/gah015;
RA Weenen C., Laven J.S., Von Bergh A.R., Cranfield M., Groome N.P.,
RA Visser J.A., Kramer P., Fauser B.C., Themmen A.P.;
RT "Anti-Muellerian hormone expression pattern in the human ovary: potential
RT implications for initial and cyclic follicle recruitment.";
RL Mol. Hum. Reprod. 10:77-83(2004).
RN [8]
RP FUNCTION, INTERACTION WITH AMHR2, AND PROTEOLYTIC PROCESSING.
RX PubMed=20861221; DOI=10.1210/me.2010-0273;
RA di Clemente N., Jamin S.P., Lugovskoy A., Carmillo P., Ehrenfels C.,
RA Picard J.Y., Whitty A., Josso N., Pepinsky R.B., Cate R.L.;
RT "Processing of anti-mullerian hormone regulates receptor activation by a
RT mechanism distinct from TGF-beta.";
RL Mol. Endocrinol. 24:2193-2206(2010).
RN [9]
RP VARIANT ARG-325.
RX PubMed=1483695; DOI=10.1007/bf00220465;
RA Carre-Eusebe D., Imbeaud S., Harbison M., New M.I., Josso N., Picard J.-Y.;
RT "Variants of the anti-Mullerian hormone gene in a compound heterozygote
RT with the persistent Mullerian duct syndrome and his family.";
RL Hum. Genet. 90:389-394(1992).
RN [10]
RP VARIANTS PMDS1 GLY-12; PRO-70; VAL-101; TRP-123; CYS-167; CYS-194 AND
RP ALA-477.
RX PubMed=8162013; DOI=10.1093/hmg/3.1.125;
RA Imbeaud S., Carre-Eusebe D., Rey R., Belville C., Josso N., Picard J.-Y.;
RT "Molecular genetics of the persistent Mullerian duct syndrome: a study of
RT 19 families.";
RL Hum. Mol. Genet. 3:125-131(1994).
RN [11]
RP VARIANTS PMDS1 GLN-506 AND TYR-525.
RX PubMed=8872466; DOI=10.1093/hmg/5.9.1269;
RA Imbeaud S., Belville C., Messika-Zeitoun L., Rey R., di Clemente N.,
RA Josso N., Picard J.-Y.;
RT "A 27 base-pair deletion of the anti-Muellerian type II receptor gene is
RT the most common cause of the persistent Muellerian duct syndrome.";
RL Hum. Mol. Genet. 5:1269-1277(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 459-560 IN COMPLEX WITH AMHR2,
RP DISULFIDE BOND, MUTAGENESIS OF ARG-472; LEU-478; GLU-481; GLN-484; LYS-534;
RP LEU-535 AND ALA-546, AND FUNCTION.
RX PubMed=34155118; DOI=10.1073/pnas.2104809118;
RA Hart K.N., Stocker W.A., Nagykery N.G., Walton K.L., Harrison C.A.,
RA Donahoe P.K., Pepin D., Thompson T.B.;
RT "Structure of AMH bound to AMHR2 provides insight into a unique signaling
RT pair in the TGF-beta family.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Plays an important role in several reproductive functions.
CC Induces Muellerian duct regression during male fetal sexual
CC differentiation (PubMed:3754790, PubMed:34155118, PubMed:8469238). Also
CC plays a role in Leydig cell differentiation and function (By
CC similarity). In female acts as a negative regulator of the primordial
CC to primary follicle transition and decreases FSH sensitivity of growing
CC follicles (PubMed:14742691). AMH signals by binding to a specific type-
CC II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1
CC and BMPR1A), and recruiting SMAD proteins that are translocated to the
CC nucleus to regulate target gene expression (PubMed:20861221,
CC PubMed:34155118). {ECO:0000250|UniProtKB:P27106,
CC ECO:0000269|PubMed:14742691, ECO:0000269|PubMed:20861221,
CC ECO:0000269|PubMed:34155118, ECO:0000269|PubMed:3754790,
CC ECO:0000269|PubMed:8469238}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:2974034,
CC ECO:0000269|PubMed:8469238}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2974034,
CC ECO:0000269|PubMed:3754790}.
CC -!- TISSUE SPECIFICITY: In ovaries, AMH is detected in granulosa cells of
CC early growing follicles. {ECO:0000269|PubMed:14742691}.
CC -!- DEVELOPMENTAL STAGE: Detected in primary follicles and continued to be
CC expressed in follicles in the antral stage. The highest level of AMH
CC expression is present in granulosa cells of secondary, preantral and
CC small antral follicles <4 mm in diameter, whereas expression is lost
CC from follicles at sizes >8 mm. {ECO:0000269|PubMed:14742691}.
CC -!- INDUCTION: Plasma AMH levels in polycystic ovary syndrome (PCOS)
CC patients are two- to threefold higher than in women with normal
CC ovaries. {ECO:0000269|PubMed:11779604}.
CC -!- PTM: Preproprotein is proteolytically processed to generate N- and C-
CC terminal cleavage products that homodimerize and associate to form a
CC biologically active non-covalent complex (PubMed:8469238,
CC PubMed:2974034). Binding of the non-covalent complex to AMHR2 induces
CC dissociation of the pro-region from the mature C-terminal dimer
CC (PubMed:20861221). The N-terminal portion of the protein, despite
CC having no intrinsic activity, has the role of amplifying the activity
CC of the C-terminus (PubMed:20861221, PubMed:8469238).
CC {ECO:0000269|PubMed:20861221, ECO:0000269|PubMed:2974034,
CC ECO:0000269|PubMed:8469238}.
CC -!- DISEASE: Persistent Muellerian duct syndrome 1 (PMDS1) [MIM:261550]: A
CC form of male pseudohermaphroditism characterized by a failure of
CC Muellerian duct regression in otherwise normal males.
CC {ECO:0000269|PubMed:8162013, ECO:0000269|PubMed:8872466}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Anti-Mullerian hormone entry;
CC URL="https://en.wikipedia.org/wiki/Anti-m%C3%BCllerian_hormone";
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DR EMBL; K03474; AAA98805.1; -; Genomic_DNA.
DR EMBL; AC005263; AAC25614.1; -; Genomic_DNA.
DR EMBL; BC049194; AAH49194.1; -; mRNA.
DR CCDS; CCDS12085.1; -.
DR PIR; A01397; WFHUM.
DR RefSeq; NP_000470.2; NM_000479.4.
DR PDB; 7L0J; X-ray; 2.60 A; A=459-560.
DR PDBsum; 7L0J; -.
DR AlphaFoldDB; P03971; -.
DR SMR; P03971; -.
DR BioGRID; 106765; 8.
DR IntAct; P03971; 4.
DR STRING; 9606.ENSP00000221496; -.
DR GlyGen; P03971; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P03971; -.
DR PhosphoSitePlus; P03971; -.
DR BioMuta; AMH; -.
DR DMDM; 313104218; -.
DR jPOST; P03971; -.
DR MassIVE; P03971; -.
DR MaxQB; P03971; -.
DR PaxDb; P03971; -.
DR PeptideAtlas; P03971; -.
DR PRIDE; P03971; -.
DR ProteomicsDB; 51624; -.
DR Antibodypedia; 22968; 548 antibodies from 32 providers.
DR DNASU; 268; -.
DR Ensembl; ENST00000221496.5; ENSP00000221496.2; ENSG00000104899.8.
DR GeneID; 268; -.
DR KEGG; hsa:268; -.
DR MANE-Select; ENST00000221496.5; ENSP00000221496.2; NM_000479.5; NP_000470.3.
DR UCSC; uc002lvh.3; human.
DR CTD; 268; -.
DR DisGeNET; 268; -.
DR GeneCards; AMH; -.
DR HGNC; HGNC:464; AMH.
DR HPA; ENSG00000104899; Group enriched (pituitary gland, testis).
DR MalaCards; AMH; -.
DR MIM; 261550; phenotype.
DR MIM; 600957; gene.
DR neXtProt; NX_P03971; -.
DR OpenTargets; ENSG00000104899; -.
DR Orphanet; 2856; Persistent Muellerian duct syndrome.
DR PharmGKB; PA24769; -.
DR VEuPathDB; HostDB:ENSG00000104899; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000006337; -.
DR HOGENOM; CLU_025681_1_0_1; -.
DR InParanoid; P03971; -.
DR OMA; DPAPLHD; -.
DR OrthoDB; 516965at2759; -.
DR PhylomeDB; P03971; -.
DR TreeFam; TF335595; -.
DR PathwayCommons; P03971; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR Reactome; R-HSA-9690406; Transcriptional regulation of testis differentiation.
DR SignaLink; P03971; -.
DR SIGNOR; P03971; -.
DR BioGRID-ORCS; 268; 12 hits in 1072 CRISPR screens.
DR GenomeRNAi; 268; -.
DR Pharos; P03971; Tbio.
DR PRO; PR:P03971; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P03971; protein.
DR Bgee; ENSG00000104899; Expressed in right hemisphere of cerebellum and 92 other tissues.
DR Genevisible; P03971; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0033327; P:Leydig cell differentiation; ISS:UniProtKB.
DR GO; GO:0001880; P:Mullerian duct regression; IDA:UniProtKB.
DR GO; GO:2000355; P:negative regulation of ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0001546; P:preantral ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007530; P:sex determination; TAS:ProtInc.
DR GO; GO:0007548; P:sex differentiation; TAS:UniProtKB.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR006799; AMH_N.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR021203; Muellerian-inhibiting_factor.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR15009; PTHR15009; 1.
DR Pfam; PF04709; AMH_N; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037270; Muellerian-inhibiting_factor; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Differentiation; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Gonadal differentiation; Growth factor;
KW Pseudohermaphroditism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2974034"
FT PROPEP 25..451
FT /evidence="ECO:0000269|PubMed:2974034"
FT /id="PRO_0000454649"
FT CHAIN 452..560
FT /note="Muellerian-inhibiting factor"
FT /id="PRO_0000033747"
FT REGION 259..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 451..452
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:2974034"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 462..526
FT /evidence="ECO:0000269|PubMed:34155118,
FT ECO:0007744|PDB:7L0J"
FT DISULFID 488..557
FT /evidence="ECO:0000269|PubMed:34155118,
FT ECO:0007744|PDB:7L0J"
FT DISULFID 492..559
FT /evidence="ECO:0000269|PubMed:34155118,
FT ECO:0007744|PDB:7L0J"
FT DISULFID 525
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:34155118"
FT VARIANT 12
FT /note="V -> G (in PMDS1; dbSNP:rs149082963)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007483"
FT VARIANT 49
FT /note="S -> I (in dbSNP:rs10407022)"
FT /evidence="ECO:0000269|PubMed:3754790"
FT /id="VAR_007484"
FT VARIANT 70
FT /note="L -> P (in PMDS1)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007485"
FT VARIANT 101
FT /note="G -> V (in PMDS1)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007486"
FT VARIANT 123
FT /note="R -> W (in PMDS1; dbSNP:rs569914235)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007487"
FT VARIANT 167
FT /note="Y -> C (in PMDS1; dbSNP:rs371874189)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007488"
FT VARIANT 185
FT /note="Q -> E (in dbSNP:rs200523942)"
FT /id="VAR_007489"
FT VARIANT 194
FT /note="R -> C (in PMDS1; dbSNP:rs777003373)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007490"
FT VARIANT 325
FT /note="Q -> R (in dbSNP:rs140765565)"
FT /evidence="ECO:0000269|PubMed:1483695"
FT /id="VAR_007491"
FT VARIANT 477
FT /note="V -> A (in PMDS1; dbSNP:rs1358787117)"
FT /evidence="ECO:0000269|PubMed:8162013"
FT /id="VAR_007492"
FT VARIANT 506
FT /note="H -> Q (in PMDS1; dbSNP:rs138571039)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_031027"
FT VARIANT 515
FT /note="V -> A (in dbSNP:rs10417628)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3754790"
FT /id="VAR_065100"
FT VARIANT 525
FT /note="C -> Y (in PMDS1)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_031028"
FT MUTAGEN 472
FT /note="R->D: Little effect on AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 478
FT /note="L->A: Abolishes AMH signaling. Does not induce
FT regression of the Muellerian duct."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 481
FT /note="E->A: Shows a slight decrease in AMH signaling.
FT Affects slightly Mullerian duct regression."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 481
FT /note="E->R,Y: Decreases AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 484
FT /note="Q->S: Little effect on AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 534
FT /note="K->A: Abolishes AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 535
FT /note="L->Y: Little effect on AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT MUTAGEN 546
FT /note="A->M: Abolishes AMH signaling."
FT /evidence="ECO:0000269|PubMed:34155118"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:7L0J"
FT HELIX 505..515
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 525..540
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 543..560
FT /evidence="ECO:0007829|PDB:7L0J"
SQ SEQUENCE 560 AA; 59195 MW; D05DCEE4FEDF94C2 CRC64;
MRDLPLTSLA LVLSALGALL GTEALRAEEP AVGTSGLIFR EDLDWPPGSP QEPLCLVALG
GDSNGSSSPL RVVGALSAYE QAFLGAVQRA RWGPRDLATF GVCNTGDRQA ALPSLRRLGA
WLRDPGGQRL VVLHLEEVTW EPTPSLRFQE PPPGGAGPPE LALLVLYPGP GPEVTVTRAG
LPGAQSLCPS RDTRYLVLAV DRPAGAWRGS GLALTLQPRG EDSRLSTARL QALLFGDDHR
CFTRMTPALL LLPRSEPAPL PAHGQLDTVP FPPPRPSAEL EESPPSADPF LETLTRLVRA
LRVPPARASA PRLALDPDAL AGFPQGLVNL SDPAALERLL DGEEPLLLLL RPTAATTGDP
APLHDPTSAP WATALARRVA AELQAAAAEL RSLPGLPPAT APLLARLLAL CPGGPGGLGD
PLRALLLLKA LQGLRVEWRG RDPRGPGRAQ RSAGATAADG PCALRELSVD LRAERSVLIP
ETYQANNCQG VCGWPQSDRN PRYGNHVVLL LKMQVRGAAL ARPPCCVPTA YAGKLLISLS
EERISAHHVP NMVATECGCR
