MXRA8_HUMAN
ID MXRA8_HUMAN Reviewed; 442 AA.
AC Q9BRK3; B3KTR6; B4DE34; Q5TA39; Q96KC3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Matrix remodeling-associated protein 8;
DE AltName: Full=Limitrin;
DE Flags: Precursor;
GN Name=MXRA8;
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).
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 [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANT
RP ASN-396.
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Pancreas;
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 [5]
RP FUNCTION, AND INTERACTION WITH ITGB3.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23386276; DOI=10.1093/cvr/cvt019;
RA Han S.W., Jung Y.K., Lee E.J., Park H.R., Kim G.W., Jeong J.H., Han M.S.,
RA Choi J.Y.;
RT "DICAM inhibits angiogenesis via suppression of AKT and p38 MAP kinase
RT signalling.";
RL Cardiovasc. Res. 98:73-82(2013).
RN [7]
RP PHOSPHORYLATION AT SER-228.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHIKUNGUNYA VIRUS
RP SPIKE GLYCOPROTEIN E2 (MICROBIAL INFECTION).
RX PubMed=29769725; DOI=10.1038/s41586-018-0121-3;
RA Zhang R., Kim A.S., Fox J.M., Nair S., Basore K., Klimstra W.B.,
RA Rimkunas R., Fong R.H., Lin H., Poddar S., Crowe J.E. Jr., Doranz B.J.,
RA Fremont D.H., Diamond M.S.;
RT "Mxra8 is a receptor for multiple arthritogenic alphaviruses.";
RL Nature 557:570-574(2018).
CC -!- FUNCTION: Transmembrane protein which can modulate activity of various
CC signaling pathways, probably via binding to integrin ITGAV:ITGB3
CC (PubMed:22492581, PubMed:23386276). Mediates heterophilic cell-cell
CC interactions in vitro (By similarity). Inhibits osteoclastogenesis
CC downstream of TNFSF11/RANKL and CSF1, where it may function by
CC attenuating signaling via integrin ITGB3 and MAP kinase p38 (By
CC similarity). Plays a role in cartilage formation where it promotes
CC proliferation and maturation of growth plate chondrocytes (By
CC similarity). Stimulates formation of primary cilia in chondrocytes (By
CC similarity). Enhances expression of genes involved in the hedgehog
CC signaling pathway in chondrocytes, including the hedgehog signaling
CC molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway
CC (By similarity). Plays a role in angiogenesis where it suppresses
CC migration of endothelial cells and also promotes their apoptosis
CC (PubMed:23386276). Inhibits VEGF-induced activation of AKT and p38 MAP
CC kinase in endothelial cells (PubMed:23386276). Also inhibits VTN
CC (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of
CC PTK2/FAK (PubMed:23386276). May play a role in the maturation and
CC maintenance of the blood-brain barrier (By similarity).
CC {ECO:0000250|UniProtKB:Q9DBV4, ECO:0000269|PubMed:22492581,
CC ECO:0000269|PubMed:23386276}.
CC -!- FUNCTION: (Microbial infection) Contributes to arthritogenic alphavirus
CC pathogenesis and acts as a receptor for these viruses.
CC {ECO:0000269|PubMed:29769725}.
CC -!- SUBUNIT: Homodimer in cis (By similarity). Does not appear to form
CC trans-homodimers (By similarity). Interacts with ITGB3; the interaction
CC inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581).
CC {ECO:0000250|UniProtKB:Q9DBV4, ECO:0000269|PubMed:22492581}.
CC -!- SUBUNIT: (Microbial infection) Interacts with chikungunya virus spike
CC glycoprotein E2. {ECO:0000269|PubMed:29769725}.
CC -!- INTERACTION:
CC Q9BRK3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-11721798, EBI-17183751;
CC Q9BRK3; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-11721798, EBI-12011224;
CC Q9BRK3; Q86UW9: DTX2; NbExp=3; IntAct=EBI-11721798, EBI-740376;
CC Q9BRK3; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-11721798, EBI-948296;
CC Q9BRK3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11721798, EBI-741158;
CC Q9BRK3; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-11721798, EBI-948354;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23386276};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q9DBV4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9DBV4}. Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q9DBV4}. Nucleus {ECO:0000269|PubMed:23386276}.
CC Note=Primarily localizes to the cell membrane (PubMed:23386276).
CC Detected in the cilium of primary chondrocytes (By similarity). Highly
CC expressed at areas of cell-cell contact and may localize to tight
CC junctions (By similarity). Also found in the nucleus where it is
CC detected in the soluble (as opposed to chromatin-bound) fraction
CC (PubMed:23386276). {ECO:0000250|UniProtKB:Q9DBV4,
CC ECO:0000269|PubMed:23386276}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BRK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRK3-2; Sequence=VSP_027448, VSP_027449;
CC Name=3;
CC IsoId=Q9BRK3-3; Sequence=VSP_054528;
CC Name=4;
CC IsoId=Q9BRK3-4; Sequence=VSP_054529;
CC -!- TISSUE SPECIFICITY: Detected in endothelial cells in mammary tissue, in
CC both large vessels (left internal mammary artery) and small capillaries
CC (vasa vasorum of the adventitia). {ECO:0000269|PubMed:23386276}.
CC -!- INDUCTION: Up-regulated in vein endothelial cells (HUVECs) in response
CC to VEGF signaling. {ECO:0000269|PubMed:23386276}.
CC -!- DOMAIN: The RGD motif is involved in integrin ITGAV:ITGB3 binding.
CC {ECO:0000250|UniProtKB:Q9DBV4}.
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DR EMBL; AB052096; BAD05132.1; -; mRNA.
DR EMBL; AK027269; BAB55010.1; -; mRNA.
DR EMBL; AK095966; BAG53178.1; -; mRNA.
DR EMBL; AK293442; BAG56945.1; -; mRNA.
DR EMBL; AL139287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006213; AAH06213.1; -; mRNA.
DR EMBL; BC017312; AAH17312.1; -; mRNA.
DR CCDS; CCDS24.1; -. [Q9BRK3-1]
DR CCDS; CCDS59950.1; -. [Q9BRK3-4]
DR CCDS; CCDS59951.1; -. [Q9BRK3-2]
DR CCDS; CCDS59952.1; -. [Q9BRK3-3]
DR RefSeq; NP_001269511.1; NM_001282582.1. [Q9BRK3-1]
DR RefSeq; NP_001269512.1; NM_001282583.1. [Q9BRK3-3]
DR RefSeq; NP_001269513.1; NM_001282584.1. [Q9BRK3-4]
DR RefSeq; NP_001269514.1; NM_001282585.1. [Q9BRK3-2]
DR RefSeq; NP_115724.1; NM_032348.3. [Q9BRK3-1]
DR PDB; 6JO8; X-ray; 3.50 A; M/N/O=25-292.
DR PDBsum; 6JO8; -.
DR AlphaFoldDB; Q9BRK3; -.
DR SMR; Q9BRK3; -.
DR BioGRID; 120064; 11.
DR IntAct; Q9BRK3; 12.
DR MINT; Q9BRK3; -.
DR STRING; 9606.ENSP00000399229; -.
DR GlyGen; Q9BRK3; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRK3; -.
DR PhosphoSitePlus; Q9BRK3; -.
DR BioMuta; MXRA8; -.
DR DMDM; 74761214; -.
DR EPD; Q9BRK3; -.
DR jPOST; Q9BRK3; -.
DR MassIVE; Q9BRK3; -.
DR MaxQB; Q9BRK3; -.
DR PaxDb; Q9BRK3; -.
DR PeptideAtlas; Q9BRK3; -.
DR PRIDE; Q9BRK3; -.
DR ProteomicsDB; 3687; -.
DR ProteomicsDB; 78776; -. [Q9BRK3-1]
DR ProteomicsDB; 78777; -. [Q9BRK3-2]
DR Antibodypedia; 66422; 19 antibodies from 8 providers.
DR DNASU; 54587; -.
DR Ensembl; ENST00000309212.11; ENSP00000307887.6; ENSG00000162576.17. [Q9BRK3-1]
DR Ensembl; ENST00000342753.8; ENSP00000344998.4; ENSG00000162576.17. [Q9BRK3-4]
DR Ensembl; ENST00000445648.5; ENSP00000399229.2; ENSG00000162576.17. [Q9BRK3-2]
DR Ensembl; ENST00000477278.3; ENSP00000436135.1; ENSG00000162576.17. [Q9BRK3-3]
DR GeneID; 54587; -.
DR KEGG; hsa:54587; -.
DR MANE-Select; ENST00000309212.11; ENSP00000307887.6; NM_032348.4; NP_115724.1.
DR UCSC; uc001aew.5; human. [Q9BRK3-1]
DR CTD; 54587; -.
DR DisGeNET; 54587; -.
DR GeneCards; MXRA8; -.
DR HGNC; HGNC:7542; MXRA8.
DR HPA; ENSG00000162576; Low tissue specificity.
DR MIM; 617293; gene.
DR neXtProt; NX_Q9BRK3; -.
DR OpenTargets; ENSG00000162576; -.
DR PharmGKB; PA31343; -.
DR VEuPathDB; HostDB:ENSG00000162576; -.
DR eggNOG; ENOG502QRZ7; Eukaryota.
DR GeneTree; ENSGT00390000001509; -.
DR HOGENOM; CLU_062248_1_0_1; -.
DR InParanoid; Q9BRK3; -.
DR OMA; DKEMQKF; -.
DR OrthoDB; 634484at2759; -.
DR PhylomeDB; Q9BRK3; -.
DR TreeFam; TF332884; -.
DR PathwayCommons; Q9BRK3; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q9BRK3; -.
DR BioGRID-ORCS; 54587; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; MXRA8; human.
DR GenomeRNAi; 54587; -.
DR Pharos; Q9BRK3; Tdark.
DR PRO; PR:Q9BRK3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BRK3; protein.
DR Bgee; ENSG00000162576; Expressed in stromal cell of endometrium and 179 other tissues.
DR Genevisible; Q9BRK3; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISS:CAFA.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; ISS:CAFA.
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; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunoglobulin domain; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Tight junction;
KW 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_0000298665"
FT TOPO_DOM 20..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..157
FT /note="Ig-like V-type 1"
FT DOMAIN 160..288
FT /note="Ig-like V-type 2"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..254
FT /note="RGD"
FT /evidence="ECO:0000250|UniProtKB:Q9DBV4"
FT SITE 325..326
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q5XI43"
FT MOD_RES 228
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 186..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..17
FT /note="MALPSRILLWKLVLLQS -> MIRCAATG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054528"
FT VAR_SEQ 25..125
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054529"
FT VAR_SEQ 407
FT /note="L -> LASSPPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027448"
FT VAR_SEQ 435..442
FT /note="GFRKENCK -> DPSGLCPLGA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027449"
FT VARIANT 396
FT /note="D -> N (in dbSNP:rs150058708)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070893"
FT CONFLICT 405
FT /note="I -> V (in Ref. 2; BAB55010)"
FT /evidence="ECO:0000305"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6JO8"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6JO8"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6JO8"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:6JO8"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:6JO8"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:6JO8"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6JO8"
SQ SEQUENCE 442 AA; 49132 MW; B08F89D726222CA1 CRC64;
MALPSRILLW KLVLLQSSAV LLHSGSSVPA AAGSSVVSES AVSWEAGARA VLRCQSPRMV
WTQDRLHDRQ RVLHWDLRGP GGGPARRLLD LYSAGEQRVY EARDRGRLEL SASAFDDGNF
SLLIRAVEET DAGLYTCNLH HHYCHLYESL AVRLEVTDGP PATPAYWDGE KEVLAVARGA
PALLTCVNRG HVWTDRHVEE AQQVVHWDRQ PPGVPHDRAD RLLDLYASGE RRAYGPLFLR
DRVAVGADAF ERGDFSLRIE PLEVADEGTY SCHLHHHYCG LHERRVFHLT VAEPHAEPPP
RGSPGNGSSH SGAPGPDPTL ARGHNVINVI VPESRAHFFQ QLGYVLATLL LFILLLVTVL
LAARRRRGGY EYSDQKSGKS KGKDVNLAEF AVAAGDQMLY RSEDIQLDYK NNILKERAEL
AHSPLPAKYI DLDKGFRKEN CK
