CADH5_MOUSE
ID CADH5_MOUSE Reviewed; 784 AA.
AC P55284; O35542;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cadherin-5;
DE AltName: Full=Vascular endothelial cadherin;
DE Short=VE-cadherin;
DE AltName: CD_antigen=CD144;
DE Flags: Precursor;
GN Name=Cdh5;
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].
RC TISSUE=Brain capillary;
RX PubMed=8555485;
RA Breier G., Breviario F., Caveda L., Berthier R., Schnuerch H., Gotsch U.,
RA Vestweber D., Risau W., Dejana E.;
RT "Molecular cloning and expression of murine vascular endothelial-cadherin
RT in early stage development of cardiovascular system.";
RL Blood 87:630-641(1996).
RN [2]
RP SEQUENCE REVISION TO 67-70.
RA Breviario F.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Mammary carcinoma;
RX PubMed=9220534;
RA Matsuyoshi N., Toda K., Horiguchi Y., Tanaka T., Nakagawa S., Takeichi M.,
RA Imamura S.;
RT "In vivo evidence of the critical role of cadherin-5 in murine vascular
RT integrity.";
RL Proc. Assoc. Am. Physicians 109:362-371(1997).
RN [4]
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 [5]
RP INTERACTION WITH PTPRB, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRB.
RX PubMed=12234928; DOI=10.1093/emboj/cdf497;
RA Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G.,
RA Golding M., Shima D.T., Deutsch U., Vestweber D.;
RT "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of
RT phosphorylation and cell contacts.";
RL EMBO J. 21:4885-4895(2002).
RN [6]
RP ERRATUM OF PUBMED:12234928.
RX DOI=10.1093/sj.emboj.cdf497;
RA Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G.,
RA Golding M., Shima D.T., Deutsch U., Vestweber D.;
RL EMBO J. 24:3158-3158(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19635461; DOI=10.1016/j.bbrc.2009.07.108;
RA Kanemura H., Satoh T., Bilasy S.E., Ueda S., Hirashima M., Kataoka T.;
RT "Impaired vascular development in the yolk sac and allantois in mice
RT lacking RA-GEF-1.";
RL Biochem. Biophys. Res. Commun. 387:754-759(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and 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 [9]
RP FUNCTION.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [10]
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22492353; DOI=10.1242/dev.071282;
RA Costa G., Mazan A., Gandillet A., Pearson S., Lacaud G., Kouskoff V.;
RT "SOX7 regulates the expression of VE-cadherin in the haemogenic endothelium
RT at the onset of haematopoietic development.";
RL Development 139:1587-1598(2012).
RN [11]
RP FUNCTION, INTERACTION WITH PALS1, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 621-ARG--ARG-623 AND 624-ILE--LYS-626.
RX PubMed=27466317; DOI=10.1091/mbc.e16-02-0127;
RA Brinkmann B.F., Steinbacher T., Hartmann C., Kummer D., Pajonczyk D.,
RA Mirzapourshafiyi F., Nakayama M., Weide T., Gerke V., Ebnet K.;
RT "VE-cadherin interacts with cell polarity protein Pals1 to regulate
RT vascular lumen formation.";
RL Mol. Biol. Cell 27:2811-2821(2016).
RN [12]
RP STRUCTURE BY NMR OF 769-784 IN COMPLEX WITH PARD3, INTERACTION WITH PARD3,
RP AND MUTAGENESIS OF TYR-774 AND ASP-777.
RX PubMed=20047332; DOI=10.1021/bi9017335;
RA Tyler R.C., Peterson F.C., Volkman B.F.;
RT "Distal interactions within the par3-VE-cadherin complex.";
RL Biochemistry 49:951-957(2010).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (By
CC similarity). They preferentially interact with themselves in a
CC homophilic manner in connecting cells; cadherins may thus contribute to
CC the sorting of heterogeneous cell types (By similarity). This cadherin
CC may play an important role in endothelial cell biology through control
CC of the cohesion and organization of the intercellular junctions
CC (PubMed:9220534, PubMed:20332120). It associates with alpha-catenin
CC forming a link to the cytoskeleton (By similarity). Acts in concert
CC with KRIT1 and PALS1 to establish and maintain correct endothelial cell
CC polarity and vascular lumen (PubMed:27466317). These effects are
CC mediated by recruitment and activation of the Par polarity complex and
CC RAP1B (By similarity). Required for activation of PRKCZ and for
CC localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the
CC cell junction (By similarity). {ECO:0000250|UniProtKB:P33151,
CC ECO:0000250|UniProtKB:Q8AYD0, ECO:0000269|PubMed:20332120,
CC ECO:0000269|PubMed:27466317, ECO:0000269|PubMed:9220534}.
CC -!- SUBUNIT: Interacts (via cadherin 5 domain) with PTPRB
CC (PubMed:12234928). Interacts with TRPC4 (By similarity). Interacts with
CC KRIT1 (By similarity). Interacts with PARD3 (PubMed:20047332).
CC Interacts with RTN4 (isoform B) (By similarity). Interacts with PALS1;
CC the interaction promotes PALS1 localization to cell junctions and is
CC required for CDH5-mediated vascular lumen formation and endothelial
CC cell polarity (PubMed:27466317). {ECO:0000250|UniProtKB:P33151,
CC ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:20047332,
CC ECO:0000269|PubMed:27466317}.
CC -!- INTERACTION:
CC P55284; Q64729: Tgfbr1; NbExp=2; IntAct=EBI-7087433, EBI-2899393;
CC P55284; Q62312: Tgfbr2; NbExp=4; IntAct=EBI-7087433, EBI-2899332;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:19635461}. Cell
CC membrane {ECO:0000269|PubMed:19635461}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:19635461}. Note=Found at cell-cell
CC boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5
CC reciprocally regulate their localization to endothelial cell-cell
CC junctions (By similarity). {ECO:0000250|UniProtKB:P33151}.
CC -!- TISSUE SPECIFICITY: Expressed in postnatal endothelial cells of the
CC retinal vascular plexus (at protein level).
CC {ECO:0000269|PubMed:27466317}.
CC -!- DEVELOPMENTAL STAGE: Expressed in endothelial cells of
CC allantois/umbilical vessels at 8.5 dpc (at protein level). During
CC hemangioblast differentiation, expressed in hemogenic endothelium cells
CC and down-regulated in nascent blood precursors.
CC {ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:22492353}.
CC -!- INDUCTION: Up-regulated by SOX7. {ECO:0000269|PubMed:22492353}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by KDR/VEGFR-2.
CC Dephosphorylated by PTPRB. {ECO:0000269|PubMed:12234928}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; X83930; CAA58782.2; -; mRNA.
DR EMBL; D63942; BAA22617.1; -; mRNA.
DR EMBL; BC054790; AAH54790.1; -; mRNA.
DR CCDS; CCDS22572.1; -.
DR RefSeq; NP_033998.2; NM_009868.4.
DR RefSeq; XP_006530693.1; XM_006530630.1.
DR PDB; 2KOH; NMR; -; B=769-784.
DR PDBsum; 2KOH; -.
DR AlphaFoldDB; P55284; -.
DR BMRB; P55284; -.
DR SMR; P55284; -.
DR BioGRID; 198640; 4.
DR CORUM; P55284; -.
DR ELM; P55284; -.
DR IntAct; P55284; 9.
DR MINT; P55284; -.
DR STRING; 10090.ENSMUSP00000034339; -.
DR GlyGen; P55284; 5 sites.
DR iPTMnet; P55284; -.
DR PhosphoSitePlus; P55284; -.
DR CPTAC; non-CPTAC-3316; -.
DR MaxQB; P55284; -.
DR PaxDb; P55284; -.
DR PeptideAtlas; P55284; -.
DR PRIDE; P55284; -.
DR ProteomicsDB; 273579; -.
DR Antibodypedia; 3717; 1245 antibodies from 43 providers.
DR DNASU; 12562; -.
DR Ensembl; ENSMUST00000034339; ENSMUSP00000034339; ENSMUSG00000031871.
DR GeneID; 12562; -.
DR KEGG; mmu:12562; -.
DR UCSC; uc009mzx.2; mouse.
DR CTD; 1003; -.
DR MGI; MGI:105057; Cdh5.
DR VEuPathDB; HostDB:ENSMUSG00000031871; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160587; -.
DR HOGENOM; CLU_005284_3_2_1; -.
DR InParanoid; P55284; -.
DR OMA; NVKFKFA; -.
DR OrthoDB; 259069at2759; -.
DR PhylomeDB; P55284; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR BioGRID-ORCS; 12562; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh5; mouse.
DR EvolutionaryTrace; P55284; -.
DR PRO; PR:P55284; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P55284; protein.
DR Bgee; ENSMUSG00000031871; Expressed in ectoplacental cone and 221 other tissues.
DR ExpressionAtlas; P55284; baseline and differential.
DR Genevisible; P55284; MM.
DR GO; GO:0005912; C:adherens junction; IDA:CAFA.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:MGI.
DR GO; GO:0034332; P:adherens junction organization; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0001955; P:blood vessel maturation; IMP:MGI.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0043114; P:regulation of vascular permeability; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0001944; P:vasculature development; IBA:GO_Central.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030052; CDH5.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF89; PTHR24027:SF89; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..45
FT /evidence="ECO:0000255"
FT /id="PRO_0000003757"
FT CHAIN 46..784
FT /note="Cadherin-5"
FT /id="PRO_0000003758"
FT TOPO_DOM 46..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..149
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 150..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 257..371
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 372..476
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 477..593
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 621..660
FT /note="Required for interaction with PALS1"
FT /evidence="ECO:0000269|PubMed:27466317"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 621..623
FT /note="RRR->AAA: Abolishes interaction with PALS1."
FT /evidence="ECO:0000269|PubMed:27466317"
FT MUTAGEN 624..626
FT /note="IRK->AAA: Abolishes interaction with PALS1."
FT /evidence="ECO:0000269|PubMed:27466317"
FT MUTAGEN 774
FT /note="Y->A: No effect on PARD3 binding."
FT /evidence="ECO:0000269|PubMed:20047332"
FT MUTAGEN 777
FT /note="D->A: Impairs PARD3 binding."
FT /evidence="ECO:0000269|PubMed:20047332"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:2KOH"
SQ SEQUENCE 784 AA; 87903 MW; 7B75698DE2F7E160 CRC64;
MQRLTELATA LGAFLGLLAV AAMAGPNFPQ IDTPNMLPAH HRQKRDWIWN QMHIDEEKNE
SLPHYVGKIK SNVNRQNAKY VLQGEFAGKI FGVDANTGNV LAYERLDREK VSEYFLTALI
VDKNTNKNLE QPSSFTVKVH DINDNWPVFS HQVFNASVPE MSAIGTSVIR VTAVDADDPT
VAGHATVLYQ IVKGNEYFSI DNSGLIFTKI KNLDREKQAE YKIVVETQDA LGLRGESGTA
TVMIRLEDIN DNFPVFTQST YTFSVPEDIR VGKPLGFLTV VDPDEPQNRM TKYSIMQGEY
RDTFTIETDP KRNEGIIKPT KSLDYEVIQQ YTFYIEATDP TIRYEYLSST SGKNKAMVTI
NVLDVDEPPV FQRHFYHFKL PENQKKPLIG TVVAKDPDKA QRSIGYSIRK TSDRGQFFRI
TKQGNIYNEK ELDRETYAWY NLTVEANELD SRGNPVGKES IVQVYIEVLD ENDNPPEFAQ
PYEPKVCENA AQGKLVVQIS ATDKDVVPVN PKFKFALKNE DSNFTLINNH DNTANITVKY
GQFNREHAKF HYLPVLISDN GVPSLTGTST LTVGVCKCNE QGEFTFCEEM AAQAGVSIQA
LVAIFLCILT ITVITLLIIL RRRIRKQAHA HSKSALEIHE QLVTYDEEGG GEMDTTSYDV
SVLNSVRGGS TKPLRSTMDA RPAVYTQVQK PPRLAPGLHG GPREMATMID VKKEEADNDG
GGPPYDTLHI YGYEGAESIA ESLSSLSTNS SDSDIDYDFL NDWGPRFKML AELYGSDPQE
ELII
