DLL1_RAT
ID DLL1_RAT Reviewed; 714 AA.
AC P97677;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Delta-like protein 1;
DE AltName: Full=Drosophila Delta homolog 1;
DE Short=Delta1;
DE Flags: Precursor;
GN Name=Dll1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Disibio G., Hebshi L., Boulter J., Weinmaster G.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION.
RX PubMed=12036964; DOI=10.1074/jbc.m204445200;
RA Panin V.M., Shao L., Lei L., Moloney D.J., Irvine K.D., Haltiwanger R.S.;
RT "Notch ligands are substrates for protein O-fucosyltransferase-1 and
RT Fringe.";
RL J. Biol. Chem. 277:29945-29952(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH EPN1.
RX PubMed=22658936; DOI=10.1016/j.devcel.2012.04.005;
RA Meloty-Kapella L., Shergill B., Kuon J., Botvinick E., Weinmaster G.;
RT "Notch ligand endocytosis generates mechanical pulling force dependent on
RT dynamin, epsins, and actin.";
RL Dev. Cell 22:1299-1312(2012).
RN [4]
RP INTERACTION WITH NOTCH1.
RX PubMed=28089369; DOI=10.1016/j.devcel.2016.12.013;
RA Kakuda S., Haltiwanger R.S.;
RT "Deciphering the fringe-mediated notch code: identification of activating
RT and inhibiting sites allowing discrimination between ligands.";
RL Dev. Cell 40:193-201(2017).
CC -!- FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3
CC receptors that binds the extracellular domain (ECD) of Notch receptor
CC in a cis and trans fashion manner (By similarity). Following
CC transinteraction, ligand cells produce mechanical force that depends of
CC a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1
CC interaction, and actin polymerisation; these events promote Notch
CC receptor extracellular domain (NECD) transendocytosis and triggers
CC Notch signaling through induction of cleavage, hyperphosphorylation,
CC and nuclear accumulation of the intracellular domain of Notch receptors
CC (NICD) (PubMed:22658936). Is required for embryonic development and
CC maintenance of adult stem cells in many different tissues and immune
CC systeme; the DLL1-induced Notch signaling is mediated through an
CC intercellular communication that regulates cell lineage, cell
CC specification, cell patterning and morphogenesis through effects on
CC differentiation and proliferation (By similarity). Plays a role in
CC brain development at different level, namely by regulating neuronal
CC differentiation of neural precursor cells via cell-cell interaction,
CC most likely through the lateral inhibitory system in an endogenous
CC level dependent-manner. During neocortex development, Dll1-Notch
CC signaling transmission is mediated by dynamic interactions between
CC intermediate neurogenic progenitors and radial glia; the cell-cell
CC interactions are mediated via dynamic and transient elongation
CC processes, likely to reactivate/maintain Notch activity in neighboring
CC progenitors, and coordinate progenitor cell division and
CC differentiation across radial and zonal boundaries. During cerebellar
CC development, regulates Bergmann glial monolayer formation and its
CC morphological maturation through a Notch signaling pathway. At the
CC retina and spinal cord level, regulates neurogenesis by preventing the
CC premature differentiation of neural progenitors and also by maintaining
CC progenitors in spinal cord through Notch signaling pathway. Also
CC controls neurogenesis of the neural tube in a progenitor domain-
CC specific fashion along the dorsoventral axis. Maintains quiescence of
CC neural stem cells and plays a role as a fate determinant that
CC segregates asymmetrically to one daughter cell during neural stem cells
CC mitosis, resulting in neuronal differentiation in Dll1-inheriting cell.
CC Plays a role in immune systeme development, namely the development of
CC all T-cells and marginal zone (MZ) B cells (By similarity). Blocks the
CC differentiation of progenitor cells into the B-cell lineage while
CC promoting the emergence of a population of cells with the
CC characteristics of a T-cell/NK-cell precursor (By similarity). Also
CC plays a role during muscle development. During early development,
CC inhibits myoblasts differentiation from the medial dermomyotomal lip
CC and later regulates progenitor cell differentiation. Directly modulates
CC cell adhesion and basal lamina formation in satellite cells through
CC Notch signaling. Maintains myogenic progenitors pool by suppressing
CC differentiation through down-regulation of MYOD1 and is required for
CC satellite cell homing and PAX7 expression. During craniofacial and
CC trunk myogenesis suppresses differentiation of cranial mesoderm-derived
CC and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-
CC derived progenitors, is neither required for satellite cell homing nor
CC for PAX7 expression. Also plays a role during pancreatic cell
CC development. During type B pancreatic cell development, may be involved
CC in the initiation of proximodistal patterning in the early pancreatic
CC epithelium. Stimulates multipotent pancreatic progenitor cells
CC proliferation and pancreatic growth by maintaining HES1 expression and
CC PTF1A protein levels. During fetal stages of development, is required
CC to maintain arterial identity and the responsiveness of arterial
CC endothelial cells for VEGFA through regulation of KDR activation and
CC NRP1 expression. Controls sprouting angiogenesis and subsequent
CC vertical branch formation througth regulation on tip cell
CC differentiation. Negatively regulates goblet cell differentiation in
CC intestine and controls secretory fat commitment through lateral
CC inhibition in small intestine. Plays a role during inner ear
CC development; negatively regulates auditory hair cell differentiation.
CC Plays a role during nephron development through Notch signaling
CC pathway. Regulates growth, blood pressure and energy homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:O00548,
CC ECO:0000250|UniProtKB:Q61483, ECO:0000269|PubMed:22658936}.
CC -!- SUBUNIT: Homodimer. Interacts with TJP1. Interacts with MAGI1 (via PDZ
CC domain); forms a complex with CTNNB1 and CDH2 and promotes recruitment
CC to the adherens junction and stabilization on the cell surface.
CC Interacts with PSEN1; undergoes a presenilin-dependent gamma-secretase
CC cleavage that releases a Dll1-intracellular form. Interacts with MFAP5.
CC Interacts with MIB1. Interacts with NEURL1B; leads to ubiquitination.
CC Interacts with NEURL1 (By similarity). Interacts with SYNJ2BP; enhances
CC DLL1 protein stability, and promotes Notch signaling in endothelial
CC cells. Interacts with MAGI1, MAGI2, MAGI3 and MPDZ (By similarity).
CC Interacts (via ubiquitin) with EPN1 (via IUM domain); binding with
CC NOTCH1 attached to neighboring cell, promotes ligand ubiquitination and
CC EPN1 interaction, leading to NECD transendocytosis and Notch signaling
CC (PubMed:22658936). Interacts with NOTCH1 (PubMed:28089369).
CC {ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:Q61483,
CC ECO:0000269|PubMed:22658936, ECO:0000269|PubMed:28089369}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q61483}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q61483}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q61483}. Membrane raft
CC {ECO:0000250|UniProtKB:Q61483}. Note=Distributed around adherens
CC junction in the apical endfeet through interactions with MAGI1.
CC {ECO:0000250|UniProtKB:Q61483}.
CC -!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis
CC and subsequent degradation (By similarity). Ubiquitinated; promotes
CC recycling back to the plasma membrane and confers a strong affinity for
CC NOTCH1. Mono- and multi-ubiquitinated. Multi-ubiquitination of LYS-605
CC by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as
CC activation of Notch signaling. Ubiquitinated by NEURL1B (By
CC similarity). {ECO:0000250|UniProtKB:P10041,
CC ECO:0000250|UniProtKB:Q61483}.
CC -!- PTM: Phosphorylated in a membrane association-dependent manner.
CC Phosphorylation at Ser-688 requires the presence of Ser-685, whereas
CC phosphorylation at Thr-630 and Ser-685 occur independently of the other
CC sites. Phosphorylation is required for full ligand activity in vitro
CC and affects surface presentation, ectodomain shedding, and endocytosis.
CC {ECO:0000250|UniProtKB:Q61483}.
CC -!- PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG.
CC {ECO:0000269|PubMed:12036964}.
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DR EMBL; U78889; AAB37343.1; -; mRNA.
DR RefSeq; NP_114452.1; NM_032063.2.
DR AlphaFoldDB; P97677; -.
DR SMR; P97677; -.
DR BioGRID; 249876; 3.
DR IntAct; P97677; 2.
DR STRING; 10116.ENSRNOP00000019934; -.
DR GlyGen; P97677; 1 site.
DR iPTMnet; P97677; -.
DR PhosphoSitePlus; P97677; -.
DR PaxDb; P97677; -.
DR GeneID; 84010; -.
DR KEGG; rno:84010; -.
DR UCSC; RGD:70949; rat.
DR CTD; 28514; -.
DR RGD; 70949; Dll1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P97677; -.
DR OrthoDB; 406049at2759; -.
DR PhylomeDB; P97677; -.
DR Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR PRO; PR:P97677; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0030957; F:Tat protein binding; ISO:RGD.
DR GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
DR GO; GO:0009912; P:auditory receptor cell fate commitment; NAS:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; TAS:RGD.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:0021688; P:cerebellar molecular layer formation; ISS:UniProtKB.
DR GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0007386; P:compartment pattern specification; ISO:RGD.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0097102; P:endothelial tip cell fate specification; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0046331; P:lateral inhibition; ISS:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; ISO:RGD.
DR GO; GO:0072070; P:loop of Henle development; ISO:RGD.
DR GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045605; P:negative regulation of epidermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; ISO:RGD.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:RGD.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; ISS:UniProtKB.
DR GO; GO:0035265; P:organ growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0072014; P:proximal tubule development; ISO:RGD.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; ISS:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0048631; P:regulation of skeletal muscle tissue growth; ISS:UniProtKB.
DR GO; GO:0014807; P:regulation of somitogenesis; ISS:UniProtKB.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISS:UniProtKB.
DR GO; GO:0048630; P:skeletal muscle tissue growth; ISS:UniProtKB.
DR GO; GO:0098773; P:skin epidermis development; ISS:UniProtKB.
DR GO; GO:0001757; P:somite specification; ISO:RGD.
DR GO; GO:0001756; P:somitogenesis; ISS:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; ISS:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; ISS:UniProtKB.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011651; Notch_ligand_N.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07657; MNNL; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Isopeptide bond; Membrane;
KW Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..714
FT /note="Delta-like protein 1"
FT /id="PRO_0000007508"
FT TOPO_DOM 18..537
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..220
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 225..253
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 256..284
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 291..324
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 331..362
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 369..401
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 408..439
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 446..477
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..515
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 644..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..714
FT /note="Interaction with MAGI1"
FT /evidence="ECO:0000250|UniProtKB:Q61483"
FT COMPBIAS 672..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 630
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61483"
FT MOD_RES 685
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q61483"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61483"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..187
FT /evidence="ECO:0000250"
FT DISULFID 191..203
FT /evidence="ECO:0000250"
FT DISULFID 211..220
FT /evidence="ECO:0000250"
FT DISULFID 225..236
FT /evidence="ECO:0000250"
FT DISULFID 229..242
FT /evidence="ECO:0000250"
FT DISULFID 244..253
FT /evidence="ECO:0000250"
FT DISULFID 256..267
FT /evidence="ECO:0000250"
FT DISULFID 262..273
FT /evidence="ECO:0000250"
FT DISULFID 275..284
FT /evidence="ECO:0000250"
FT DISULFID 291..303
FT /evidence="ECO:0000250"
FT DISULFID 297..313
FT /evidence="ECO:0000250"
FT DISULFID 315..324
FT /evidence="ECO:0000250"
FT DISULFID 331..342
FT /evidence="ECO:0000250"
FT DISULFID 336..351
FT /evidence="ECO:0000250"
FT DISULFID 353..362
FT /evidence="ECO:0000250"
FT DISULFID 369..380
FT /evidence="ECO:0000250"
FT DISULFID 374..390
FT /evidence="ECO:0000250"
FT DISULFID 392..401
FT /evidence="ECO:0000250"
FT DISULFID 408..419
FT /evidence="ECO:0000250"
FT DISULFID 413..428
FT /evidence="ECO:0000250"
FT DISULFID 430..439
FT /evidence="ECO:0000250"
FT DISULFID 446..457
FT /evidence="ECO:0000250"
FT DISULFID 451..466
FT /evidence="ECO:0000250"
FT DISULFID 468..477
FT /evidence="ECO:0000250"
FT DISULFID 484..495
FT /evidence="ECO:0000250"
FT DISULFID 489..504
FT /evidence="ECO:0000250"
FT DISULFID 506..515
FT /evidence="ECO:0000250"
FT CROSSLNK 605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61483"
SQ SEQUENCE 714 AA; 77379 MW; 4B8EE2272BAEA27E CRC64;
MGRRSALALA VVSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGSG PPCACRTFFR
VCLKHYQASV SPEPPCTYGS AVTAVLGVDS FSLPDGAGID PAFSNPIRFP FGFTWPGTFS
LIIEALHTDS PDDLATENPE RLISRLTTQR HLTVGEEWSQ DLHSSGRTDL RYSYRFVCDE
HYYGEGCSVF CRPRDDAFGH FTCGERGEKM CDPGWKGQYC TDPICLPGCD DQHGYCDKPG
ECKCRVGWQG RYCDECIRYP GCLHGTCQQP WQCNCQEGWG GLFCNQDLNY CTHHKPCRNG
ATCTNTGQGS YTCSCRPGYT GANCELEVDE CAPSPCRNGG SCTDLEDSYS CTCPPGFYGK
VCELSAMTCA DGPCFNGGRC SDNPDGGYTC HCPAGFSGFN CEKKIDLCSS SPCSNGAKCV
DLGNSYLCRC QTGFSGRYCE DNVDDCASSP CANGGTCRDS VNDFSCTCPP GYTGRNCSAP
VSRCEHAPCH NGATCHQRGQ RYMCECAQGY GGANCQFLLP EPPPDLIVAA QGGSFPWVAV
CAGVVLVLLL LLGCAAVVVC VRLKLQKHQP PPDPCGGETE TMNNLANCQR EKDVSVSIIG
ATQIKNTNKK ADFHGDHGAD KSSFKARYPT VDYNLIRDLK GDEATVRDAH SKRDTKCQSQ
GSVGEEKSTS TLRGGEVPDR KRPESVYSTS KDTKYQSVYV LSAEKDECVI ATEV
