EXPH5_HUMAN
ID EXPH5_HUMAN Reviewed; 1989 AA.
AC Q8NEV8; Q2KHM1; Q9Y4D6;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Exophilin-5 {ECO:0000305};
DE AltName: Full=Synaptotagmin-like protein homolog lacking C2 domains b;
DE Short=SlaC2-b;
DE Short=Slp homolog lacking C2 domains b;
GN Name=EXPH5 {ECO:0000312|HGNC:HGNC:30578}; Synonyms=KIAA0624, SLAC2B;
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), POSSIBLE FUNCTION, AND VARIANTS
RP GLY-19; ASN-676 AND ARG-1663.
RC TISSUE=Placenta;
RX PubMed=12062444; DOI=10.1016/s0014-5793(02)02634-0;
RA Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
RA Izumi T.;
RT "Melanophilin directly links Rab27a and myosin Va through its distinct
RT coiled-coil regions.";
RL FEBS Lett. 517:233-238(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASN-676
RP AND ARG-1663.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-19;
RP ASN-676 AND ARG-1663.
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 TISSUE SPECIFICITY, AND INVOLVEMENT IN EBNS.
RX PubMed=23176819; DOI=10.1016/j.ajhg.2012.10.012;
RA McGrath J.A., Stone K.L., Begum R., Simpson M.A., Dopping-Hepenstal P.J.,
RA Liu L., McMillan J.R., South A.P., Pourreyron C., McLean W.H.,
RA Martinez A.E., Mellerio J.E., Parsons M.;
RT "Germline mutation in EXPH5 implicates the Rab27B effector protein SlaC2-b
RT in inherited skin fragility.";
RL Am. J. Hum. Genet. 91:1115-1121(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-806; SER-809;
RP SER-1028; SER-1086; SER-1124; SER-1505; SER-1753; SER-1768; SER-1821 AND
RP SER-1851, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1753, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC trafficking.
CC -!- SUBUNIT: Interacts with RAB27A. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NEV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEV8-2; Sequence=VSP_007906;
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes.
CC {ECO:0000269|PubMed:23176819}.
CC -!- DISEASE: Epidermolysis bullosa, non-specific, autosomal recessive
CC (EBNS) [MIM:615028]: A skin disease characterized by blistering of skin
CC and mucosae, following minimal pressure or trauma. Various clinical
CC types with different severity are recognized, ranging from severe
CC mutilating forms to mild forms with limited and localized scarring, and
CC less frequent extracutaneous manifestations. EBNS clinical features
CC mainly comprise trauma-induced scale crusts and intermittent skin
CC blistering. Some of the crusted areas are hemorrhagic and accompanied
CC by occasional bruising. Most lesions clear over several weeks to leave
CC slightly atrophic scars and moderate post-inflammatory
CC hyperpigmentation. {ECO:0000269|PubMed:23176819}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31599.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY099469; AAM44402.1; -; mRNA.
DR EMBL; AB014524; BAA31599.1; ALT_INIT; mRNA.
DR EMBL; AP000871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113119; AAI13120.1; -; mRNA.
DR CCDS; CCDS76473.1; -. [Q8NEV8-2]
DR CCDS; CCDS8341.1; -. [Q8NEV8-1]
DR PIR; T00385; T00385.
DR RefSeq; NP_001294948.1; NM_001308019.1.
DR AlphaFoldDB; Q8NEV8; -.
DR IntAct; Q8NEV8; 9.
DR MINT; Q8NEV8; -.
DR STRING; 9606.ENSP00000265843; -.
DR GlyGen; Q8NEV8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NEV8; -.
DR PhosphoSitePlus; Q8NEV8; -.
DR BioMuta; EXPH5; -.
DR DMDM; 296439360; -.
DR EPD; Q8NEV8; -.
DR jPOST; Q8NEV8; -.
DR MassIVE; Q8NEV8; -.
DR MaxQB; Q8NEV8; -.
DR PaxDb; Q8NEV8; -.
DR PeptideAtlas; Q8NEV8; -.
DR PRIDE; Q8NEV8; -.
DR ProteomicsDB; 73221; -. [Q8NEV8-1]
DR ProteomicsDB; 73222; -. [Q8NEV8-2]
DR Antibodypedia; 54955; 54 antibodies from 15 providers.
DR DNASU; 23086; -.
DR Ensembl; ENST00000265843.9; ENSP00000265843.4; ENSG00000110723.12. [Q8NEV8-1]
DR Ensembl; ENST00000525344.5; ENSP00000432546.1; ENSG00000110723.12. [Q8NEV8-2]
DR GeneID; 23086; -.
DR KEGG; hsa:23086; -.
DR MANE-Select; ENST00000265843.9; ENSP00000265843.4; NM_015065.3; NP_055880.2.
DR UCSC; uc001pkk.3; human. [Q8NEV8-1]
DR CTD; 23086; -.
DR DisGeNET; 23086; -.
DR GeneCards; EXPH5; -.
DR GeneReviews; EXPH5; -.
DR HGNC; HGNC:30578; EXPH5.
DR HPA; ENSG00000110723; Group enriched (brain, skin).
DR MalaCards; EXPH5; -.
DR MIM; 612878; gene.
DR MIM; 615028; phenotype.
DR neXtProt; NX_Q8NEV8; -.
DR OpenTargets; ENSG00000110723; -.
DR Orphanet; 412189; Epidermolysis bullosa simplex due to exophilin 5 deficiency.
DR VEuPathDB; HostDB:ENSG00000110723; -.
DR eggNOG; ENOG502RVAY; Eukaryota.
DR GeneTree; ENSGT00390000011087; -.
DR HOGENOM; CLU_001683_0_0_1; -.
DR InParanoid; Q8NEV8; -.
DR PhylomeDB; Q8NEV8; -.
DR TreeFam; TF335662; -.
DR PathwayCommons; Q8NEV8; -.
DR SignaLink; Q8NEV8; -.
DR BioGRID-ORCS; 23086; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; EXPH5; human.
DR GenomeRNAi; 23086; -.
DR Pharos; Q8NEV8; Tbio.
DR PRO; PR:Q8NEV8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NEV8; protein.
DR Bgee; ENSG00000110723; Expressed in tongue squamous epithelium and 176 other tissues.
DR ExpressionAtlas; Q8NEV8; baseline and differential.
DR Genevisible; Q8NEV8; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0003334; P:keratinocyte development; IMP:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR InterPro; IPR039916; EXPH5.
DR InterPro; IPR010911; Rab_BD.
DR PANTHER; PTHR21469; PTHR21469; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Epidermolysis bullosa; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1989
FT /note="Exophilin-5"
FT /id="PRO_0000190230"
FT DOMAIN 7..63
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..1989
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..10
FT /note="MTKVPPAFDF -> MSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_007906"
FT VARIANT 19
FT /note="R -> G (in dbSNP:rs2640738)"
FT /evidence="ECO:0000269|PubMed:12062444,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030538"
FT VARIANT 118
FT /note="R -> L (in dbSNP:rs3741046)"
FT /id="VAR_030539"
FT VARIANT 137
FT /note="E -> V (in dbSNP:rs2640785)"
FT /id="VAR_030540"
FT VARIANT 328
FT /note="R -> Q (in dbSNP:rs11212684)"
FT /id="VAR_030541"
FT VARIANT 512
FT /note="M -> L (in dbSNP:rs17108127)"
FT /id="VAR_030542"
FT VARIANT 525
FT /note="V -> F (in dbSNP:rs12146448)"
FT /id="VAR_030543"
FT VARIANT 676
FT /note="S -> N (in dbSNP:rs2846412)"
FT /evidence="ECO:0000269|PubMed:12062444,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_030544"
FT VARIANT 777
FT /note="D -> N (in dbSNP:rs3741048)"
FT /id="VAR_030545"
FT VARIANT 853
FT /note="L -> P (in dbSNP:rs10749920)"
FT /id="VAR_030546"
FT VARIANT 892
FT /note="N -> Y (in dbSNP:rs10890850)"
FT /id="VAR_030547"
FT VARIANT 899
FT /note="V -> A (in dbSNP:rs17108112)"
FT /id="VAR_030548"
FT VARIANT 1147
FT /note="M -> I (in dbSNP:rs34012545)"
FT /id="VAR_057117"
FT VARIANT 1236
FT /note="S -> A (in dbSNP:rs35520914)"
FT /id="VAR_057118"
FT VARIANT 1240
FT /note="D -> N (in dbSNP:rs11828459)"
FT /id="VAR_030549"
FT VARIANT 1311
FT /note="C -> R (in dbSNP:rs877474)"
FT /id="VAR_030550"
FT VARIANT 1343
FT /note="T -> A (in dbSNP:rs34978242)"
FT /id="VAR_057119"
FT VARIANT 1656
FT /note="E -> K (in dbSNP:rs35083468)"
FT /id="VAR_057120"
FT VARIANT 1663
FT /note="G -> R (in dbSNP:rs2640779)"
FT /evidence="ECO:0000269|PubMed:12062444,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_030551"
FT VARIANT 1735
FT /note="I -> F (in dbSNP:rs35717245)"
FT /id="VAR_057121"
FT VARIANT 1967
FT /note="D -> N (in dbSNP:rs1943382)"
FT /evidence="ECO:0000269|PubMed:12062444,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_030552"
SQ SEQUENCE 1989 AA; 222520 MW; DE36430AD569628F CRC64;
MTKVPPAFDF SFLNDEEARK ILQVLERNEE LQRAEKDRIS KLQKTKRDIR WLQGVTGEWF
EEIQRKKFCN ETDVSQMLKQ PLTYRLSKEM AKNDPIELPT SRSKNVTNQK KPTPFSSRMS
FRSSFASLFS FRKSGKETSK LPSLGQKGCD GHAGPPMPVR GAAVQAKIYN SPLENHLVDS
TFVPKPAVMR EESGMPPPWD ASLLENEFFQ VLDDLDSKLA QEQSASSVNT RTPLNYGSRT
QFGHFYSSGN RHGNITERHK KHYNETSNMS IYDILRPGTP REGFKTFSPR TSTIYDMYRT
REPRVFKEDY VQKNTFGSTS LCFDSRQRSA LPATGHFTAR SLHFPATTQS KSGFIPPRHQ
QSPKRTPLSS IIWNRSDSSR DRENQEEFLR APSPMEIDPA DKYVYPRGFQ ENKRYESYHS
QNVYQRVSLN APMENAMSPD TFENSENMPF YHQSNTFTRS FFSNTFGRSG EQRRFGQGPF
WGQEKGHSFW SDFHRSRKSF SSSDRDFEMI SMEANSVSAI HGHNVSSEHW ESFSSGYGTD
VSRGQEEPHP WQFDFQRSTL DSMVVSHGNE TQLTPHFGTP NVCSMTGSSY HVKSSELVSQ
QDSSPVEVHI NKEASSFGIA QTLASSFKTS FSQISDDRRN PQSPNLQNPT VTLQKIFPNK
PASHPMRSHT EVTVTSSNSV DSLPLAKSQP NILVTEVNNE KDLNESISEE DKQLSKMDQT
NKAGEIPQPV SQTGISNSLP DFQNPLSQDS AKSNGFGFNA STIISSKKSP RVFSRKDTSK
MYIPHTDKSN DIKQDKRFTE NRKLGSTASL PFIQEHRTPP SFPRTDQGCH QELTVNNEDI
SRIITNNHWS SALTDTQNAQ YSKCKLTPGH KTSCDSLDLS SAALPDSSPS KNSSLDAPVV
PSTTVFSRRS PSDKDPSLGE REEKDNAGKN QKNQFIVSHS ENQERNDSPV PTHDEVVDVK
CHSHSPFRNE RGKGKIRHHI SCIEKLSKTE SISVPTSDHR SLIEANQSNS KVSELDTIYC
TLPRKSSSFL IHGRQSGSKI MAASLRNGPP PFQIKNNVED AMGNYMLNKF SPSSPESANE
CSKVLSDSAL EAPEATERMT NVKSSGSTSV RKGPLPFLIN RAMSCPSGEP HASTGREGRK
KPLTSGMDAS ELTPRAWERI ISPVESDSSV RDCSLTKRQH QKENFQEYTE KEGKMAASRR
SVFALSNEDP LPFCSDLSGK ERGKTLHKVK TTSTFSVSGD EDNVKCLEVV SIYYTLPRKP
SKKFCNLLQQ YTQNTNLLIE SPQVETETFP NALEKDKQNY STREQSGTPS CENLKMSVNS
DQTLTTENMT AFRLSNRGPL APTLQEMASV EAAVSLPEEE SKAREIFSDN LAKTPLGDSE
NKKERGKKLQ SETLHTSLML QRKNVSEEKS ENCQQSINSS NSGPSSLPAL SEVNIGNSQT
RRSSWECTGS GRAIPFTGSG KCPQKDHTST AVGDGSSGSQ PREGRGDIGT NCQKMTNKTL
SHSESQVFAL TPALHKLQLG EETQSDEPNL ESLQSEPREL PQRSQEANMT ESRKAEDEMQ
KSAWDQPSLP EGNKNKTNLD DLVKGENRSS VKHRLAAMSK ASRKFPAKDV SPRRHVATIF
PQSGSRSGFD HLSLGTVECN PLFPEPTPKS AESIGESRLS ENGKHVKKSE NLLPITVLPN
REPSTHVSNQ KSNSISQRHQ NEFKNVSESP SKHENSKDVT AAQNLVRESG APSPITFTSL
REAEFSDNQR RLSPPFPLEP AQKSRVSSPL ASFLQQQRSA SSLEWEPEPH LYRSKSLKSI
NVHGDLLRKS HPPKVRERHF SESTSIDNAL SRLTLGNEFS VNNGYSRRFR SFSELPSCDG
NESWAYRSGT KTGPRSAISI YRPIDYGIFG KEQQLAFLEN VKRSLTQGRL WKPSFLKNPG
FLKDDLRNPP NPSESLSSNS PSSQVPEDGL SPSEPLNIYE DDPVDSDCDT DTTTDDEYYL
DENDKESEL
