MXRA8_MOUSE
ID MXRA8_MOUSE Reviewed; 442 AA.
AC Q9DBV4; Q76M97; Q920S7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Matrix remodeling-associated protein 8 {ECO:0000312|MGI:MGI:1922011};
DE AltName: Full=Adipocyte-specific protein 3 {ECO:0000312|EMBL:BAB68501.1};
DE AltName: Full=Dual Ig domain-containing cell adhesion molecule {ECO:0000303|PubMed:18366072};
DE Short=DICAM {ECO:0000303|PubMed:18366072};
DE AltName: Full=Limitrin {ECO:0000303|PubMed:14603461};
DE Flags: Precursor;
GN Name=Mxra8 {ECO:0000312|MGI:MGI:1922011};
GN Synonyms=Asp3 {ECO:0000312|EMBL:BAB68501.1},
GN Dicam {ECO:0000303|PubMed:18366072};
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], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=14603461; DOI=10.1002/glia.10279;
RA Yonezawa T., Ohtsuka A., Yoshitaka T., Hirano S., Nomoto H., Yamamoto K.,
RA Ninomiya Y.;
RT "Limitrin, a novel immunoglobulin superfamily protein localized to glia
RT limitans formed by astrocyte endfeet.";
RL Glia 44:190-204(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsuruga H.;
RT "Adipocyte-specific protein 3, a novel protein upregulated during adipocyte
RT differentiation.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MOTIF RGD, AND
RP MUTAGENESIS OF ASP-130 AND ASP-253.
RX PubMed=18366072; DOI=10.1002/jcp.21438;
RA Jung Y.K., Jin J.S., Jeong J.H., Kim H.N., Park N.R., Choi J.Y.;
RT "DICAM, a novel dual immunoglobulin domain containing cell adhesion
RT molecule interacts with alphavbeta3 integrin.";
RL J. Cell. Physiol. 216:603-614(2008).
RN [7]
RP FUNCTION, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=22492581; DOI=10.1002/jbmr.1632;
RA Jung Y.K., Han S.W., Kim G.W., Jeong J.H., Kim H.J., Choi J.Y.;
RT "DICAM inhibits osteoclast differentiation through attenuation of the
RT integrin alphaVbeta3 pathway.";
RL J. Bone Miner. Res. 27:2024-2034(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=29702220; DOI=10.1016/j.joca.2018.04.008;
RA Han S., Park H.R., Lee E.J., Jang J.A., Han M.S., Kim G.W., Jeong J.H.,
RA Choi J.Y., Beier F., Jung Y.K.;
RT "Dicam promotes proliferation and maturation of chondrocyte through Indian
RT hedgehog signaling in primary cilia.";
RL Osteoarthritis Cartilage 26:945-953(2018).
CC -!- FUNCTION: Transmembrane protein which can modulate activity of various
CC signaling pathways, probably via binding to integrin ITGAV:ITGB3
CC (PubMed:18366072, PubMed:22492581, PubMed:29702220). Mediates
CC heterophilic cell-cell interactions in vitro (PubMed:18366072).
CC Inhibits osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where
CC it may function by attenuating signaling via integrin ITGB3 and MAP
CC kinase p38 (PubMed:22492581). Plays a role in cartilage formation where
CC it promotes proliferation and maturation of growth plate chondrocytes
CC (PubMed:29702220). Stimulates formation of primary cilia in
CC chondrocytes (PubMed:29702220). Enhances expression of genes involved
CC in the hedgehog signaling pathway in chondrocytes, including the
CC hedgehog signaling molecule IHH; may also promote signaling via the
CC PTHLH/PTHrP pathway (PubMed:29702220). Plays a role in angiogenesis
CC where it suppresses migration of endothelial cells and also promotes
CC their apoptosis (By similarity). Inhibits VEGF-induced activation of
CC AKT and p38 MAP kinase in endothelial cells (By similarity). Also
CC inhibits VTN (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and
CC activation of PTK2/FAK (By similarity). May play a role in the
CC maturation and maintenance of the blood-brain barrier
CC (PubMed:14603461). {ECO:0000250|UniProtKB:Q9BRK3,
CC ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072,
CC ECO:0000269|PubMed:22492581, ECO:0000269|PubMed:29702220}.
CC -!- SUBUNIT: Homodimer in cis (PubMed:18366072). Does not appear to form
CC trans-homodimers (PubMed:18366072). Interacts with ITGB3; the
CC interaction inhibits ITGAV:ITGB3 heterodimer formation
CC (PubMed:22492581). {ECO:0000269|PubMed:18366072,
CC ECO:0000269|PubMed:22492581}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14603461,
CC ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581}; Single-pass
CC type I membrane protein {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000269|PubMed:18366072}. Cytoplasm {ECO:0000269|PubMed:18366072,
CC ECO:0000269|PubMed:29702220}. Cell projection, cilium membrane
CC {ECO:0000269|PubMed:29702220}. Nucleus {ECO:0000269|PubMed:18366072}.
CC Note=Primarily localizes to the cell membrane (PubMed:18366072).
CC Detected in the cilium of primary chondrocytes (PubMed:29702220).
CC Highly expressed at areas of cell-cell contact and may localize to
CC tight junctions (PubMed:18366072). Also found in the nucleus where it
CC is detected in the soluble (as opposed to chromatin-bound) fraction
CC (PubMed:18366072). {ECO:0000269|PubMed:18366072,
CC ECO:0000269|PubMed:29702220}.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level)
CC (PubMed:18366072). Highly expressed in brain where it localizes to the
CC glia limitans, which is formed by the endfeet of astrocytes surrounding
CC capillaries, and beneath the pia mater (at protein level)
CC (PubMed:14603461). In lung, detected in epithelial cells of the
CC bronchus (at protein level). Expressed in intercalated disks in the
CC heart (at protein level) (PubMed:18366072). Detected in pancreatic
CC alpha-cells in the islet of Langerhans (at protein level)
CC (PubMed:18366072). In kidney, found in the brush border of the proximal
CC convoluted tubule (at protein level) (PubMed:18366072). Expressed in
CC the epithelium of the small intestine (at protein level)
CC (PubMed:18366072). Weakly expressed in liver (at protein level)
CC (PubMed:18366072). Detected in myeloid cells (PubMed:22492581).
CC {ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072,
CC ECO:0000269|PubMed:22492581}.
CC -!- DEVELOPMENTAL STAGE: At embryonic stage 15.5 dpc, expressed in the
CC growth plate of long bones where it is mostly found in chondrocytes in
CC the resting and proliferative zones (at protein level)
CC (PubMed:29702220). Expression gradually increases in differentiating
CC osteoclasts, but then decreases during the late stages of
CC differentiation (PubMed:22492581). {ECO:0000269|PubMed:22492581,
CC ECO:0000269|PubMed:29702220}.
CC -!- INDUCTION: Disruption of the blood-brain barrier by cold injury results
CC in a drastic reduction in expression (PubMed:14603461). Up-regulated in
CC primary chondrocytes in response to BMP2 and PTHLH/PTHrP
CC (PubMed:29702220). {ECO:0000269|PubMed:14603461,
CC ECO:0000269|PubMed:29702220}.
CC -!- DOMAIN: RGD motif 2 (but not RGD motif 1) is involved in integrin
CC ITGAV:ITGB3 binding. {ECO:0000269|PubMed:18366072}.
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DR EMBL; AB052097; BAD05133.1; -; mRNA.
DR EMBL; AB040488; BAB68501.1; -; mRNA.
DR EMBL; AK004732; BAB23514.1; -; mRNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026438; AAH26438.1; -; mRNA.
DR CCDS; CCDS19044.1; -.
DR RefSeq; NP_077225.4; NM_024263.4.
DR PDB; 6JO7; X-ray; 2.40 A; A/B=23-291.
DR PDB; 6NK3; X-ray; 2.20 A; A/B=23-296.
DR PDB; 6NK6; EM; 4.06 A; M/N/O/P=32-299.
DR PDB; 6NK7; EM; 4.99 A; N=32-292.
DR PDBsum; 6JO7; -.
DR PDBsum; 6NK3; -.
DR PDBsum; 6NK6; -.
DR PDBsum; 6NK7; -.
DR AlphaFoldDB; Q9DBV4; -.
DR SMR; Q9DBV4; -.
DR BioGRID; 217001; 5.
DR STRING; 10090.ENSMUSP00000030947; -.
DR GlyConnect; 2503; 1 N-Linked glycan (1 site).
DR GlyGen; Q9DBV4; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9DBV4; -.
DR PhosphoSitePlus; Q9DBV4; -.
DR SwissPalm; Q9DBV4; -.
DR MaxQB; Q9DBV4; -.
DR PaxDb; Q9DBV4; -.
DR PRIDE; Q9DBV4; -.
DR ProteomicsDB; 293591; -.
DR Antibodypedia; 66422; 19 antibodies from 8 providers.
DR Ensembl; ENSMUST00000030947; ENSMUSP00000030947; ENSMUSG00000029070.
DR GeneID; 74761; -.
DR KEGG; mmu:74761; -.
DR UCSC; uc012dqy.1; mouse.
DR CTD; 54587; -.
DR MGI; MGI:1922011; Mxra8.
DR VEuPathDB; HostDB:ENSMUSG00000029070; -.
DR eggNOG; ENOG502QRZ7; Eukaryota.
DR GeneTree; ENSGT00390000001509; -.
DR InParanoid; Q9DBV4; -.
DR OMA; DKEMQKF; -.
DR OrthoDB; 634484at2759; -.
DR PhylomeDB; Q9DBV4; -.
DR TreeFam; TF332884; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 74761; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9DBV4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DBV4; protein.
DR Bgee; ENSMUSG00000029070; Expressed in vault of skull and 251 other tissues.
DR ExpressionAtlas; Q9DBV4; baseline and differential.
DR Genevisible; Q9DBV4; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR013106; Ig_V-set.
DR InterPro; IPR042472; MXRA8.
DR PANTHER; PTHR44793; PTHR44793; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..442
FT /note="Matrix remodeling-associated protein 8"
FT /id="PRO_0000298666"
FT TOPO_DOM 20..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..156
FT /note="Ig-like V-type 1"
FT DOMAIN 159..291
FT /note="Ig-like V-type 2"
FT REGION 296..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..130
FT /note="RGD 1"
FT /evidence="ECO:0000305|PubMed:18366072"
FT MOTIF 251..253
FT /note="RGD 2"
FT /evidence="ECO:0000305|PubMed:18366072"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 324..325
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q5XI43"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK3"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 185..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 130
FT /note="D->E: No significant effect on integrin ITGAV:ITGB3
FT binding."
FT /evidence="ECO:0000269|PubMed:18366072"
FT MUTAGEN 253
FT /note="D->E: Reduced integrin ITGAV:ITGB3 binding."
FT /evidence="ECO:0000269|PubMed:18366072"
FT CONFLICT 33
FT /note="S -> N (in Ref. 1; BAD05133, 2; BAB68501 and 5;
FT AAH26438)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> D (in Ref. 1; BAD05133)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> E (in Ref. 1; BAD05133, 2; BAB68501 and 5;
FT AAH26438)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> D (in Ref. 1; BAD05133)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="Y -> H (in Ref. 1; BAD05133, 2; BAB68501 and 5;
FT AAH26438)"
FT /evidence="ECO:0000305"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6NK3"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6JO7"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6NK3"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6NK3"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6NK3"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6NK3"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:6NK3"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:6NK3"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:6NK3"
SQ SEQUENCE 442 AA; 49750 MW; 9600816B14AAA6EF CRC64;
MELLSRVLLW KLLLLQSSAV LSSGPSGTAA ASSSLVSESV VSLAAGTQAV LRCQSPRMVW
TQDRLHDRQR VVHWDLSGGP GSQRRRLVDM YSAGEQRVYE PRDRDRLLLS PSAFHDGNFS
LLIRAVDRGD EGVYTCNLHH HYCHLDESLA VRLEVTEDPL LSRAYWDGEK EVLVVAHGAP
ALMTCINRAH VWTDRHLEEA QQVVHWDRQL PGVSHDRADR LLDLYASGER RAYGPPFLRD
RVSVNTNAFA RGDFSLRIDE LERADEGIYS CHLHHHYCGL HERRVFHLQV TEPAFEPPAR
ASPGNGSGHS SAPSPDPTLT RGHSIINVIV PEDHTHFFQQ LGYVLATLLL FILLLITVVL
ATRYRHSGGC KTSDKKAGKS KGKDVNMVEF AVATRDQAPY RTEDIQLDYK NNILKERAEL
AHSPLPAKDV DLDKEFRKEY CK
