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EXOC5_HUMAN
ID   EXOC5_HUMAN             Reviewed;         708 AA.
AC   O00471; B2R6C5; Q8IW24;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Exocyst complex component 5;
DE   AltName: Full=Exocyst complex component Sec10;
DE            Short=hSec10;
GN   Name=EXOC5; Synonyms=SEC10, SEC10L1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9119050; DOI=10.1016/s0014-5793(97)00109-9;
RA   Guo W., Roth D., Gatti E., De Camilli P., Novick P.;
RT   "Identification and characterization of homologues of the exocyst component
RT   Sec10p.";
RL   FEBS Lett. 404:135-139(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus;
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].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   SUBCELLULAR LOCATION.
RX   PubMed=18756269; DOI=10.1038/emboj.2008.166;
RA   Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M.,
RA   Camonis J.;
RT   "Distinct roles of RalA and RalB in the progression of cytokinesis are
RT   supported by distinct RalGEFs.";
RL   EMBO J. 27:2375-2387(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC       EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1
CC       (By similarity). {ECO:0000250|UniProtKB:P97878,
CC       ECO:0000250|UniProtKB:Q3TPX4}.
CC   -!- INTERACTION:
CC       O00471; A0AVN2: BARD1; NbExp=3; IntAct=EBI-949824, EBI-9977322;
CC       O00471; Q99728: BARD1; NbExp=3; IntAct=EBI-949824, EBI-473181;
CC       O00471; P23560-2: BDNF; NbExp=3; IntAct=EBI-949824, EBI-12275524;
CC       O00471; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-949824, EBI-5666615;
CC       O00471; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-949824, EBI-747505;
CC       O00471; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-949824, EBI-10171570;
CC       O00471; P02511: CRYAB; NbExp=3; IntAct=EBI-949824, EBI-739060;
CC       O00471; P53674: CRYBB1; NbExp=3; IntAct=EBI-949824, EBI-7519424;
CC       O00471; Q05D60: DEUP1; NbExp=11; IntAct=EBI-949824, EBI-748597;
CC       O00471; Q3B7T1-5: EDRF1; NbExp=3; IntAct=EBI-949824, EBI-10240074;
CC       O00471; Q6FHV6: ENO2; NbExp=3; IntAct=EBI-949824, EBI-10249724;
CC       O00471; Q8TAG9: EXOC6; NbExp=6; IntAct=EBI-949824, EBI-1223394;
CC       O00471; Q9Y2D4: EXOC6B; NbExp=6; IntAct=EBI-949824, EBI-2690026;
CC       O00471; P02671-2: FGA; NbExp=3; IntAct=EBI-949824, EBI-9640259;
CC       O00471; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-949824, EBI-741729;
CC       O00471; P04406: GAPDH; NbExp=3; IntAct=EBI-949824, EBI-354056;
CC       O00471; Q8N4P3: HDDC3; NbExp=3; IntAct=EBI-949824, EBI-750003;
CC       O00471; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-949824, EBI-16429135;
CC       O00471; O14964: HGS; NbExp=3; IntAct=EBI-949824, EBI-740220;
CC       O00471; P42858: HTT; NbExp=3; IntAct=EBI-949824, EBI-466029;
CC       O00471; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-949824, EBI-725672;
CC       O00471; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-949824, EBI-14069005;
CC       O00471; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-949824, EBI-739657;
CC       O00471; P43357: MAGEA3; NbExp=3; IntAct=EBI-949824, EBI-5651459;
CC       O00471; P43360: MAGEA6; NbExp=6; IntAct=EBI-949824, EBI-1045155;
CC       O00471; P00973: OAS1; NbExp=3; IntAct=EBI-949824, EBI-3932815;
CC       O00471; P00973-2: OAS1; NbExp=6; IntAct=EBI-949824, EBI-12081862;
CC       O00471; D3DTS7: PMP22; NbExp=3; IntAct=EBI-949824, EBI-25882629;
CC       O00471; A0A0S2Z528: PSTPIP1; NbExp=3; IntAct=EBI-949824, EBI-16430249;
CC       O00471; Q13882: PTK6; NbExp=6; IntAct=EBI-949824, EBI-1383632;
CC       O00471; Q9ULZ3: PYCARD; NbExp=5; IntAct=EBI-949824, EBI-751215;
CC       O00471; P61106: RAB14; NbExp=6; IntAct=EBI-949824, EBI-1056404;
CC       O00471; P20338: RAB4A; NbExp=6; IntAct=EBI-949824, EBI-722284;
CC       O00471; P61018: RAB4B; NbExp=6; IntAct=EBI-949824, EBI-10218066;
CC       O00471; P37840: SNCA; NbExp=3; IntAct=EBI-949824, EBI-985879;
CC       O00471; Q96E40: SPACA9; NbExp=3; IntAct=EBI-949824, EBI-722584;
CC       O00471; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-949824, EBI-5235340;
CC       O00471; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-949824, EBI-357085;
CC       O00471; Q13148: TARDBP; NbExp=6; IntAct=EBI-949824, EBI-372899;
CC       O00471; Q96FV9: THOC1; NbExp=3; IntAct=EBI-949824, EBI-1765605;
CC       O00471; O14787: TNPO2; NbExp=4; IntAct=EBI-949824, EBI-431907;
CC       O00471; Q86WV8: TSC1; NbExp=3; IntAct=EBI-949824, EBI-12806590;
CC       O00471; Q6PF05-3: TTC23L; NbExp=3; IntAct=EBI-949824, EBI-10182647;
CC       O00471; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-949824, EBI-6116822;
CC       O00471; P83876: TXNL4A; NbExp=3; IntAct=EBI-949824, EBI-746539;
CC       O00471; O75604: USP2; NbExp=3; IntAct=EBI-949824, EBI-743272;
CC       O00471; O76024: WFS1; NbExp=3; IntAct=EBI-949824, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119050}. Midbody
CC       {ECO:0000269|PubMed:18756269}. Note=Localization at the midbody
CC       requires the presence of RALA, EXOC2 and EXOC3.
CC       {ECO:0000269|PubMed:18756269}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9119050}.
CC   -!- SIMILARITY: Belongs to the SEC10 family. {ECO:0000305}.
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DR   EMBL; U85946; AAB53388.1; -; mRNA.
DR   EMBL; AK312523; BAG35422.1; -; mRNA.
DR   EMBL; CH471061; EAW80699.1; -; Genomic_DNA.
DR   EMBL; BC041126; AAH41126.1; -; mRNA.
DR   CCDS; CCDS45111.1; -.
DR   RefSeq; NP_006535.1; NM_006544.3.
DR   AlphaFoldDB; O00471; -.
DR   SMR; O00471; -.
DR   BioGRID; 115884; 120.
DR   ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR   ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR   CORUM; O00471; -.
DR   IntAct; O00471; 87.
DR   MINT; O00471; -.
DR   STRING; 9606.ENSP00000484855; -.
DR   TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR   iPTMnet; O00471; -.
DR   PhosphoSitePlus; O00471; -.
DR   BioMuta; EXOC5; -.
DR   EPD; O00471; -.
DR   jPOST; O00471; -.
DR   MassIVE; O00471; -.
DR   MaxQB; O00471; -.
DR   PaxDb; O00471; -.
DR   PeptideAtlas; O00471; -.
DR   PRIDE; O00471; -.
DR   ProteomicsDB; 47919; -.
DR   Antibodypedia; 24095; 127 antibodies from 26 providers.
DR   DNASU; 10640; -.
DR   Ensembl; ENST00000621441.5; ENSP00000484855.1; ENSG00000070367.16.
DR   GeneID; 10640; -.
DR   KEGG; hsa:10640; -.
DR   MANE-Select; ENST00000621441.5; ENSP00000484855.1; NM_006544.4; NP_006535.1.
DR   UCSC; uc001xct.4; human.
DR   CTD; 10640; -.
DR   DisGeNET; 10640; -.
DR   GeneCards; EXOC5; -.
DR   HGNC; HGNC:10696; EXOC5.
DR   HPA; ENSG00000070367; Low tissue specificity.
DR   MIM; 604469; gene.
DR   neXtProt; NX_O00471; -.
DR   OpenTargets; ENSG00000070367; -.
DR   PharmGKB; PA35619; -.
DR   VEuPathDB; HostDB:ENSG00000070367; -.
DR   eggNOG; KOG3745; Eukaryota.
DR   GeneTree; ENSGT00390000012837; -.
DR   HOGENOM; CLU_020771_1_0_1; -.
DR   InParanoid; O00471; -.
DR   OMA; PLCKHHY; -.
DR   OrthoDB; 225235at2759; -.
DR   PhylomeDB; O00471; -.
DR   TreeFam; TF314966; -.
DR   PathwayCommons; O00471; -.
DR   Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR   Reactome; R-HSA-264876; Insulin processing.
DR   Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR   SignaLink; O00471; -.
DR   BioGRID-ORCS; 10640; 344 hits in 1074 CRISPR screens.
DR   ChiTaRS; EXOC5; human.
DR   GeneWiki; EXOC5; -.
DR   GenomeRNAi; 10640; -.
DR   Pharos; O00471; Tbio.
DR   PRO; PR:O00471; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; O00471; protein.
DR   Bgee; ENSG00000070367; Expressed in cortical plate and 193 other tissues.
DR   ExpressionAtlas; O00471; baseline and differential.
DR   Genevisible; O00471; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR   GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR   GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR   GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR   InterPro; IPR033960; EXOC5/Sec10.
DR   InterPro; IPR009976; Sec10-like.
DR   PANTHER; PTHR12100; PTHR12100; 1.
DR   PANTHER; PTHR12100:SF4; PTHR12100:SF4; 1.
DR   Pfam; PF07393; Sec10; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Exocytosis; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..708
FT                   /note="Exocyst complex component 5"
FT                   /id="PRO_0000118943"
FT   COILED          40..101
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         122
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         395
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97878"
FT   MOD_RES         405
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97878"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97878"
FT   VARIANT         10
FT                   /note="E -> D (in dbSNP:rs35132458)"
FT                   /id="VAR_048957"
FT   CONFLICT        545
FT                   /note="G -> R (in Ref. 4; AAH41126)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   708 AA;  81853 MW;  CB03AC6C64DAB50C CRC64;
     MATTAELFEE PFVADEYIER LVWRTPGGGS RGGPEAFDPK RLLEEFVNHI QELQIMDERI
     QRKVEKLEQQ CQKEAKEFAK KVQELQKSNQ VAFQHFQELD EHISYVATKV CHLGDQLEGV
     NTPRQRAVEA QKLMKYFNEF LDGELKSDVF TNSEKIKEAA DIIQKLHLIA QELPFDRFSE
     VKSKIASKYH DLECQLIQEF TSAQRRGEIS RMREVAAVLL HFKGYSHCVD VYIKQCQEGA
     YLRNDIFEDA GILCQRVNKQ VGDIFSNPET VLAKLIQNVF EIKLQSFVKE QLEECRKSDA
     EQYLKNLYDL YTRTTNLSSK LMEFNLGTDK QTFLSKLIKS IFISYLENYI EVETGYLKSR
     SAMILQRYYD SKNHQKRSIG TGGIQDLKER IRQRTNLPLG PSIDTHGETF LSQEVVVNLL
     QETKQAFERC HRLSDPSDLP RNAFRIFTIL VEFLCIEHID YALETGLAGI PSSDSRNANL
     YFLDVVQQAN TIFHLFDKQF NDHLMPLISS SPKLSECLQK KKEIIEQMEM KLDTGIDRTL
     NCMIGQMKHI LAAEQKKTDF KPEDENNVLI QYTNACVKVC AYVRKQVEKI KNSMDGKNVD
     TVLMELGVRF HRLIYEHLQQ YSYSCMGGML AICDVAEYRK CAKDFKIPMV LHLFDTLHAL
     CNLLVVAPDN LKQVCSGEQL ANLDKNILHS FVQLRADYRS ARLARHFS
 
 
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