TMEDA_RAT
ID TMEDA_RAT Reviewed; 219 AA.
AC Q63584; Q9R0W6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transmembrane emp24 domain-containing protein 10;
DE Short=Protein Tmed10;
DE AltName: Full=21 kDa transmembrane-trafficking protein;
DE AltName: Full=Transmembrane protein Tmp21;
DE AltName: Full=p24 family protein delta-1;
DE Short=p24delta1;
DE Flags: Precursor;
GN Name=Tmed10 {ECO:0000312|PROSITE:PS50866}; Synonyms=Tmp21;
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].
RC TISSUE=Pancreas;
RX PubMed=10376215; DOI=10.3109/10425179909008429;
RA Hoerer J., Blum R., Feick P., Nastainczyk W., Schulz I.;
RT "A comparative study of rat and human Tmp21 (p23) reveals the pseudogene-
RT like features of human Tmp21-II.";
RL DNA Seq. 10:121-126(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-219, TISSUE SPECIFICITY, AND INTERACTION
RP WITH TMED2.
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=8663407; DOI=10.1074/jbc.271.29.17183;
RA Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R., Nastainczyk W.,
RA Schulz I.;
RT "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal
RT membranes, are members of a protein family involved in vesicular
RT trafficking.";
RL J. Biol. Chem. 271:17183-17189(1996).
RN [3]
RP PROTEIN SEQUENCE OF 32-47, INTERACTION WITH TMED2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9472029; DOI=10.1083/jcb.140.4.751;
RA Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P.,
RA Thomas D.Y., Bergeron J.J., Nilsson T.;
RT "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both
RT COP I and II coatomer.";
RL J. Cell Biol. 140:751-765(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TMED2.
RX PubMed=10214941; DOI=10.1016/s0014-5793(99)00246-x;
RA Gommel D., Orci L., Emig E.M., Hannah M.J., Ravazzola M., Nickel W.,
RA Helms J.B., Wieland F.T., Sohn K.;
RT "p24 and p23, the major transmembrane proteins of COPI-coated transport
RT vesicles, form hetero-oligomeric complexes and cycle between the organelles
RT of the early secretory pathway.";
RL FEBS Lett. 447:179-185(1999).
RN [5]
RP INTERACTION WITH KDELR2; TMED2 AND ARF1.
RX PubMed=11703931; DOI=10.1016/s1534-5807(01)00004-1;
RA Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
RT "KDEL-cargo regulates interactions between proteins involved in COPI
RT vesicle traffic: measurements in living cells using FRET.";
RL Dev. Cell 1:139-153(2001).
RN [6]
RP METHYLATION AT ARG-171 AND ARG-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA Yates J.R. III, Howell K.E.;
RT "Organellar proteomics reveals Golgi arginine dimethylation.";
RL Mol. Biol. Cell 15:2907-2919(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15718469; DOI=10.1126/science.1108061;
RA Malsam J., Satoh A., Pelletier L., Warren G.;
RT "Golgin tethers define subpopulations of COPI vesicles.";
RL Science 307:1095-1098(2005).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF 215-LYS-LYS-216.
RX PubMed=18627576; DOI=10.1111/j.1600-0854.2008.00784.x;
RA Blum R., Lepier A.;
RT "The luminal domain of p23 (Tmp21) plays a critical role in p23 cell
RT surface trafficking.";
RL Traffic 9:1530-1550(2008).
RN [9]
RP INTERACTION WITH STX17.
RX PubMed=21545355; DOI=10.1042/bc20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain
RT the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=31455601; DOI=10.1242/bio.045336;
RA Del Olmo T., Lacarriere-Keita C., Normandin C., Jean D., Boisvert F.M.,
RA Jean S.;
RT "RAB21 interacts with TMED10 and modulates its localization and
RT abundance.";
RL Biol. Open 8:0-0(2019).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 12-132, FUNCTION IN TRANSPORT OF
RP GPI-ANCHORED PROTEINS, AND INTERACTION WITH TMED2.
RX PubMed=27569046; DOI=10.1016/j.jmb.2016.08.023;
RA Nagae M., Hirata T., Morita-Matsumoto K., Theiler R., Fujita M.,
RA Kinoshita T., Yamaguchi Y.;
RT "3D structure and interaction of p24beta and p24delta golgi dynamics
RT domains: implication for p24 complex formation and cargo transport.";
RL J. Mol. Biol. 428:4087-4099(2016).
CC -!- FUNCTION: Cargo receptor involved in protein vesicular trafficking and
CC quality control in the endoplasmic reticulum (ER) and Golgi (By
CC similarity). The p24 protein family is a group of transmembrane
CC proteins that bind coat protein complex I/COPI and coat protein complex
CC II/COPII involved in vesicular trafficking between the membranes (By
CC similarity). Acts at the lumenal side for incorporation of secretory
CC cargo molecules into transport vesicles and involved in vesicle coat
CC formation at the cytoplasmic side (PubMed:10214941). Mainly functions
CC in the early secretory pathway and cycles between the ER, ER-Golgi
CC intermediate compartment (ERGIC) and Golgi, mediating cargo transport
CC through COPI and COPII-coated vesicles (PubMed:10214941). In COPII
CC vesicle-mediated anterograde transport, involved in the transport of
CC GPI-anchored proteins by acting together with TMED2 as their cargo
CC receptor; the function specifically implies SEC24C and SEC24D of the
CC COPII vesicle coat and lipid raft-like microdomains of the ER
CC (PubMed:27569046). Recognizes GPI anchors structural remodeled in the
CC ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase
CC MPPE1/PGAP5 (PubMed:27569046). In COPI vesicle-mediated retrograde
CC transport, involved in the biogenesis of COPI vesicles and vesicle coat
CC recruitment. Involved in trafficking of amyloid beta A4 protein and
CC soluble APP-beta release (independent from the modulation of gamma-
CC secretase activity) (By similarity). Involved in the KDELR2-mediated
CC retrograde transport of the toxin A subunit (CTX-A-K63)together with
CC COPI and the COOH terminus of KDELR2 (By similarity). On Golgi
CC membranes, acts as primary receptor for ARF1-GDP, a GTP-binding protein
CC involved in COPI-vesicle formation. Increases coatomer-dependent
CC GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of
CC ARF1-bound GTP and therefore modulates protein trafficking from the
CC Golgi apparatus. Involved in the exocytic trafficking of G protein-
CC coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme
CC receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor)
CC from the Golgi to the plasma membrane, thus contributing to receptor
CC resensitization. In addition to its cargo receptor activity, may also
CC act as a protein channel after oligomerization, facilitating the post-
CC translational entry of leaderless cytoplasmic cargo into the ERGIC.
CC Involved in the translocation into ERGIC, the vesicle entry and the
CC secretion of leaderless cargos (lacking the secretion signal sequence),
CC including the mature form of interleukin 1/IL-1 family members, the
CC alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins
CC galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated
CC protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process
CC is dependent on cargo protein unfolding and enhanced by chaperones
CC HSP90AB1 and HSP90B1/GRP9. Could also associates with the presenilin-
CC dependent gamma-secretase complex in order to regulate gamma-cleavages
CC of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (By
CC similarity). {ECO:0000250|UniProtKB:P49755,
CC ECO:0000250|UniProtKB:Q28735, ECO:0000269|PubMed:10214941,
CC ECO:0000269|PubMed:27569046}.
CC -!- SUBUNIT: Predominantly dimeric and to a lesser extent monomeric in the
CC ER. Monomer and dimer in ERGIC and cis-Golgi network. Forms
CC homooligomer (via GOLD domain); the assembly is promoted by direct
CC binding with leaderless cargos and may form a protein channel that
CC facilitates cargo entry into the ERGIC (By similarity). Forms
CC heterooligomeric complexes with other members of the p24 family such as
CC TMED2, TMED7 and TMED9 (PubMed:8663407, PubMed:10214941,
CC PubMed:11703931). Interacts (via GOLD domain) with TMED2 (via GOLD
CC domain); the complex is required for export of TMED10 from the ER to
CC the cis-Golgi network; the complex is proposed to be involved in cis-
CC Golgi network dynamics and / or biogenesis (PubMed:27569046).
CC Associates with the COPI vesicle coat subunits (coatomer) (By
CC similarity). Tetramerization of the cytoplasmic domain at the Golgi
CC membrane in vitro; the complex is proposed to interact with COPI
CC coatomer and induce budding of the vesicles (By similarity). Interacts
CC with COPG1; the interaction involves TMED10 homodimer (By similarity).
CC Interacts with ARF1 (GDP-bound); the interaction probably involves a
CC TMED10 oligomer (PubMed:11703931). Interacts with SEC23A, SEC24B,
CC SEC24C and SEC24D components of the coat protein complex II/COPII,
CC indicative of an association of TMED10 with the COPII vesicle coat.
CC Interacts with CD59 (PubMed:9472029). Interacts with MPPE1/PGAP5; the
CC complex might recruit and sort GPI-anchored proteins to the ER-exit
CC site, or the interaction might lead to recycling of PGAP5 between the
CC ER and the Golgi. Interacts with F2LR1/PAR2 (By similarity). Interacts
CC with KDELR2/ERD2; the interaction is disrupted by KDELR2 ligand
CC (PubMed:11703931). Found in a complex composed at least of SURF4, TMED2
CC and TMED10 (By similarity). Associates with the presenilin-dependent
CC gamma-secretase complex. Interacts with STX17; the interaction is
CC direct (By similarity). Interacts with IL-1; the interaction is direct
CC (PubMed:21545355). Interacts with RAB21 (active GTP-bound form); the
CC interaction is indirect and regulates TMED10 abundance and localization
CC at the Golgi (By similarity). {ECO:0000250|UniProtKB:P49755,
CC ECO:0000250|UniProtKB:Q28735, ECO:0000269|PubMed:10214941,
CC ECO:0000269|PubMed:11703931, ECO:0000269|PubMed:21545355,
CC ECO:0000269|PubMed:27569046, ECO:0000269|PubMed:8663407,
CC ECO:0000269|PubMed:9472029}.
CC -!- INTERACTION:
CC Q63584; Q9R064: Gorasp2; NbExp=2; IntAct=EBI-918648, EBI-4422912;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:P49755}; Single-pass type I membrane
CC protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10214941, ECO:0000269|PubMed:15718469,
CC ECO:0000269|PubMed:18627576, ECO:0000269|PubMed:9472029}; Single-pass
CC type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000269|PubMed:18627576,
CC ECO:0000269|PubMed:31455601, ECO:0000269|PubMed:9472029}; Single-pass
CC type I membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000269|PubMed:31455601}; Single-pass type I
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:P49755}; Single-pass type I membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18627576};
CC Single-pass type I membrane protein {ECO:0000255}. Melanosome
CC {ECO:0000250|UniProtKB:P49755}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8663407}.
CC -!- DOMAIN: The GOLD domain is required for proper p24 heterooligomeric
CC complex formation and efficient transport of GPI-anchored proteins.
CC {ECO:0000269|PubMed:27569046}.
CC -!- DOMAIN: The lumenal domain mediates localization to the plasma membrane
CC by partially overriding the ER retention by the cytoplasmic domain.
CC {ECO:0000269|PubMed:18627576}.
CC -!- MISCELLANEOUS: Ectopic expression of TMED10 alone does not result in
CC its proper cis-Golgi network localization. Interaction of TMED10 with
CC TMED2 is both necessary and sufficient for transport of the couple to
CC the cis-Golgi network, and TMED3 and/or TMED9 contribute to
CC facilitating the process. {ECO:0000250|UniProtKB:P49755}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AJ004912; CAA06212.1; -; mRNA.
DR EMBL; X97443; CAA66072.1; -; mRNA.
DR RefSeq; NP_445919.1; NM_053467.1.
DR PDB; 5AZX; X-ray; 1.58 A; A/B/C/D=32-132.
DR PDB; 5AZY; X-ray; 1.80 A; A/B=32-132.
DR PDBsum; 5AZX; -.
DR PDBsum; 5AZY; -.
DR AlphaFoldDB; Q63584; -.
DR SMR; Q63584; -.
DR BioGRID; 250029; 1.
DR IntAct; Q63584; 8.
DR STRING; 10116.ENSRNOP00000010512; -.
DR GlyGen; Q63584; 1 site.
DR iPTMnet; Q63584; -.
DR PhosphoSitePlus; Q63584; -.
DR SwissPalm; Q63584; -.
DR jPOST; Q63584; -.
DR PaxDb; Q63584; -.
DR PRIDE; Q63584; -.
DR GeneID; 84599; -.
DR KEGG; rno:84599; -.
DR UCSC; RGD:620970; rat.
DR CTD; 10972; -.
DR RGD; 620970; Tmed10.
DR VEuPathDB; HostDB:ENSRNOG00000007901; -.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_1_1; -.
DR InParanoid; Q63584; -.
DR OMA; AMGNDYH; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q63584; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q63584; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007901; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q63584; RN.
DR GO; GO:0005801; C:cis-Golgi network; IDA:HGNC-UCL.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:RGD.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:HGNC-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:HGNC-UCL.
DR GO; GO:0008320; F:protein transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0035964; P:COPI-coated vesicle budding; ISS:UniProtKB.
DR GO; GO:0106273; P:cytosol to ERGIC protein transport; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0106272; P:protein localization to ERGIC; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IEP:HGNC-UCL.
DR GO; GO:1902003; P:regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; NAS:HGNC-UCL.
DR GO; GO:0048199; P:vesicle targeting, to, from or within Golgi; IEP:HGNC-UCL.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Glycoprotein; Golgi apparatus; Membrane; Methylation; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..219
FT /note="Transmembrane emp24 domain-containing protein 10"
FT /id="PRO_0000010404"
FT TOPO_DOM 32..185
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18627576"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18627576"
FT DOMAIN 41..193
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..142
FT /note="Required for interaction with STX17"
FT /evidence="ECO:0000250"
FT REGION 147..178
FT /note="Required for TMED10 and TMED2 cis-Golgi network
FT localization"
FT /evidence="ECO:0000250"
FT REGION 204..219
FT /note="Interaction with COPG1"
FT /evidence="ECO:0000250"
FT REGION 207..219
FT /note="Interaction with ARF1 and IL1B"
FT /evidence="ECO:0000250|UniProtKB:P49755"
FT MOTIF 211..219
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 211..212
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 171
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT MOD_RES 176
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 215..216
FT /note="KK->SS: Reduced localization to COPI-coated vesicles
FT and endoplasmic reticulum-Golgi intermediate compartment."
FT /evidence="ECO:0000269|PubMed:18627576"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:5AZX"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:5AZX"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5AZX"
SQ SEQUENCE 219 AA; 24858 MW; 51FC99ECB6D47ADE CRC64;
MSGLSGPLSW PGPLLSALLF LFLLGPSSVL GISFHLPVNS RKCLREEIHK DLLVTGAYEI
TDQSGGAGGL RTHLKITDSA GHILYAKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE
STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE
