MDGA1_HUMAN
ID MDGA1_HUMAN Reviewed; 955 AA.
AC Q8NFP4; A6NHG0; Q8NBE3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 1;
DE AltName: Full=GPI and MAM protein;
DE Short=GPIM;
DE AltName: Full=Glycosylphosphatidylinositol-MAM;
DE AltName: Full=MAM domain-containing protein 3;
DE Flags: Precursor;
GN Name=MDGA1; Synonyms=MAMDC3;
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 [MRNA] (ISOFORM 1).
RX PubMed=12082541; DOI=10.1038/sj.onc.1205383;
RA De Juan C., Iniesta P., Gonzalez-Quevedo R., Moran A., Sanchez-Pernaute A.,
RA Torres A.J., Balibrea J.L., Diaz-Rubio E., Cruces J., Benito M.;
RT "Genomic organization of a novel glycosylphosphatidylinositol MAM gene
RT expressed in human tissues and tumors.";
RL Oncogene 21:3089-3094(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-955 (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=15922729; DOI=10.1016/j.yexcr.2005.02.016;
RA Diaz-Lopez A., Rivas C., Iniesta P., Moran A., Garcia-Aranda C., Megias D.,
RA Sanchez-Pernaute A., Torres A., Diaz-Rubio E., Benito M., De Juan C.;
RT "Characterization of MDGA1, a novel human glycosylphosphatidylinositol-
RT anchored protein localized in lipid rafts.";
RL Exp. Cell Res. 307:91-99(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-247.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH NLGN2.
RX PubMed=23248271; DOI=10.1073/pnas.1219987110;
RA Lee K., Kim Y., Lee S.-J., Qiang Y., Lee D., Lee H.W., Kim H., Je H.S.,
RA Suedhof T.C., Ko J.;
RT "MDGAs interact selectively with neuroligin-2 but not other neuroligins to
RT regulate inhibitory synapse development.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:336-341(2013).
RN [8]
RP VARIANT SER-935.
RX PubMed=27607563; DOI=10.1111/cge.12850;
RA Mahmud A.A., Nahid N.A., Nassif C., Sayeed M.S., Ahmed M.U., Parveen M.,
RA Khalil M.I., Islam M.M., Nahar Z., Rypens F., Hamdan F.F., Rouleau G.A.,
RA Hasnat A., Michaud J.L.;
RT "Loss of the proprioception and touch sensation channel PIEZO2 in siblings
RT with a progressive form of contractures.";
RL Clin. Genet. 91:470-475(2017).
CC -!- FUNCTION: Required for radial migration of cortical neurons in the
CC superficial layer of the neocortex (By similarity). Plays a role in the
CC formation or maintenance of inhibitory synapses. May function by
CC inhibiting the activity of NLGN2. {ECO:0000250,
CC ECO:0000269|PubMed:23248271}.
CC -!- SUBUNIT: Interacts heterophilically through its MAM domain with
CC proteins in axon-rich regions and through its Ig-like domains with
CC proteins in differentiating muscle (By similarity). Interacts (through
CC the Ig-like domains) with NLGN2. {ECO:0000250,
CC ECO:0000269|PubMed:23248271}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15922729};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15922729}. Note=Associated
CC with lipid rafts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NFP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFP4-2; Sequence=VSP_009835;
CC -!- TISSUE SPECIFICITY: Has been found in brain, heart, skeletal muscle and
CC kidney. Found to be overexpressed in tumor tissues.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF478693; AAM77220.1; -; mRNA.
DR EMBL; AL049553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03952.1; -; Genomic_DNA.
DR EMBL; AK090677; BAC03502.1; ALT_INIT; mRNA.
DR CCDS; CCDS47417.1; -. [Q8NFP4-1]
DR RefSeq; NP_705691.1; NM_153487.3. [Q8NFP4-1]
DR RefSeq; XP_006715119.1; XM_006715056.3. [Q8NFP4-2]
DR PDB; 5V5V; X-ray; 4.11 A; G/H/I/J/K/L=22-237.
DR PDB; 5V5W; X-ray; 2.72 A; A=22-237.
DR PDB; 5XEQ; X-ray; 3.14 A; B=19-330.
DR PDBsum; 5V5V; -.
DR PDBsum; 5V5W; -.
DR PDBsum; 5XEQ; -.
DR AlphaFoldDB; Q8NFP4; -.
DR SMR; Q8NFP4; -.
DR BioGRID; 129333; 3.
DR STRING; 9606.ENSP00000402584; -.
DR GlyGen; Q8NFP4; 11 sites.
DR iPTMnet; Q8NFP4; -.
DR PhosphoSitePlus; Q8NFP4; -.
DR BioMuta; MDGA1; -.
DR DMDM; 46396459; -.
DR EPD; Q8NFP4; -.
DR MassIVE; Q8NFP4; -.
DR PaxDb; Q8NFP4; -.
DR PeptideAtlas; Q8NFP4; -.
DR PRIDE; Q8NFP4; -.
DR ProteomicsDB; 73330; -. [Q8NFP4-1]
DR ProteomicsDB; 73331; -. [Q8NFP4-2]
DR Antibodypedia; 29838; 30 antibodies from 13 providers.
DR DNASU; 266727; -.
DR Ensembl; ENST00000434837.8; ENSP00000402584.2; ENSG00000112139.17. [Q8NFP4-1]
DR Ensembl; ENST00000505425.5; ENSP00000422042.1; ENSG00000112139.17. [Q8NFP4-2]
DR GeneID; 266727; -.
DR KEGG; hsa:266727; -.
DR MANE-Select; ENST00000434837.8; ENSP00000402584.2; NM_153487.4; NP_705691.1.
DR UCSC; uc003onu.2; human. [Q8NFP4-1]
DR CTD; 266727; -.
DR DisGeNET; 266727; -.
DR GeneCards; MDGA1; -.
DR HGNC; HGNC:19267; MDGA1.
DR HPA; ENSG00000112139; Tissue enriched (brain).
DR MIM; 609626; gene.
DR neXtProt; NX_Q8NFP4; -.
DR OpenTargets; ENSG00000112139; -.
DR PharmGKB; PA134864540; -.
DR VEuPathDB; HostDB:ENSG00000112139; -.
DR eggNOG; ENOG502QUWH; Eukaryota.
DR GeneTree; ENSGT00940000159201; -.
DR HOGENOM; CLU_014908_0_0_1; -.
DR InParanoid; Q8NFP4; -.
DR OMA; SMRNATF; -.
DR OrthoDB; 118847at2759; -.
DR PhylomeDB; Q8NFP4; -.
DR TreeFam; TF330345; -.
DR PathwayCommons; Q8NFP4; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 266727; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; MDGA1; human.
DR GenomeRNAi; 266727; -.
DR Pharos; Q8NFP4; Tbio.
DR PRO; PR:Q8NFP4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NFP4; protein.
DR Bgee; ENSG00000112139; Expressed in cardiac muscle of right atrium and 158 other tissues.
DR ExpressionAtlas; Q8NFP4; baseline and differential.
DR Genevisible; Q8NFP4; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0007420; P:brain development; ISS:HGNC-UCL.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; ISS:HGNC-UCL.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..932
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 1"
FT /id="PRO_0000014864"
FT PROPEP 933..955
FT /note="Removed in mature form"
FT /id="PRO_0000292042"
FT DOMAIN 24..123
FT /note="Ig-like 1"
FT DOMAIN 132..230
FT /note="Ig-like 2"
FT DOMAIN 240..323
FT /note="Ig-like 3"
FT DOMAIN 338..432
FT /note="Ig-like 4"
FT DOMAIN 440..532
FT /note="Ig-like 5"
FT DOMAIN 539..631
FT /note="Ig-like 6"
FT DOMAIN 643..743
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 751..918
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 779..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 932
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 357..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 463..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 560..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 926..955
FT /note="VVVMPGSGAPCQSSPQLWGPMAIFLLALQR -> GARREGGGGAESGGSCAW
FT RGFLSVEGGCLGLNRGSECLSDGNHVALTV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009835"
FT VARIANT 61
FT /note="L -> P (in dbSNP:rs10947690)"
FT /id="VAR_047660"
FT VARIANT 935
FT /note="P -> S (in dbSNP:rs368283829)"
FT /evidence="ECO:0000269|PubMed:27607563"
FT /id="VAR_077845"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5V5W"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5V5W"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 118..129
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:5V5W"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:5V5W"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5V5W"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:5XEQ"
SQ SEQUENCE 955 AA; 105790 MW; BD41A1EB10A05962 CRC64;
MEVTCLLLLA LIPFHCRGQG VYAPAQAQIV HAGQACVVKE DNISERVYTI REGDTLMLQC
LVTGHPRPQV RWTKTAGSAS DKFQETSVFN ETLRIERIAR TQGGRYYCKA ENGVGVPAIK
SIRVDVQYLD EPMLTVHQTV SDVRGNFYQE KTVFLRCTVN SNPPARFIWK RGSDTLSHSQ
DNGVDIYEPL YTQGETKVLK LKNLRPQDYA SYTCQVSVRN VCGIPDKAIT FRLTNTTAPP
ALKLSVNETL VVNPGENVTV QCLLTGGDPL PQLQWSHGPG PLPLGALAQG GTLSIPSVQA
RDSGYYNCTA TNNVGNPAKK TVNLLVRSMK NATFQITPDV IKESENIQLG QDLKLSCHVD
AVPQEKVTYQ WFKNGKPARM SKRLLVTRND PELPAVTSSL ELIDLHFSDY GTYLCMASFP
GAPVPDLSVE VNISSETVPP TISVPKGRAV VTVREGSPAE LQCEVRGKPR PPVLWSRVDK
EAALLPSGLP LEETPDGKLR LERVSRDMSG TYRCQTARYN GFNVRPREAQ VQLNVQFPPE
VEPSSQDVRQ ALGRPVLLRC SLLRGSPQRI ASAVWRFKGQ LLPPPPVVPA AAEAPDHAEL
RLDAVTRDSS GSYECSVSND VGSAACLFQV SAKAYSPEFY FDTPNPTRSH KLSKNYSYVL
QWTQREPDAV DPVLNYRLSI RQLNQHNAVV KAIPVRRVEK GQLLEYILTD LRVPHSYEVR
LTPYTTFGAG DMASRIIHYT EPINSPNLSD NTCHFEDEKI CGYTQDLTDN FDWTRQNALT
QNPKRSPNTG PPTDISGTPE GYYMFIETSR PRELGDRARL VSPLYNASAK FYCVSFFYHM
YGKHIGSLNL LVRSRNKGAL DTHAWSLSGN KGNVWQQAHV PISPSGPFQI IFEGVRGPGY
LGDIAIDDVT LKKGECPRKQ TDPNKVVVMP GSGAPCQSSP QLWGPMAIFL LALQR
