PLXA1_HUMAN
ID PLXA1_HUMAN Reviewed; 1896 AA.
AC Q9UIW2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Plexin-A1;
DE AltName: Full=Semaphorin receptor NOV;
DE Flags: Precursor;
GN Name=PLXNA1; Synonyms=NOV, PLXN1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-1776, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8570614; DOI=10.1073/pnas.93.2.674;
RA Maestrini E., Tamagnone L., Longati P., Cremona O., Gulisano M., Bione S.,
RA Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.;
RT "A family of transmembrane proteins with homology to the MET-hepatocyte
RT growth factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:674-678(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1622-1896.
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77 AND ASN-1043.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
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).
CC -!- FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary
CC for signaling by class 3 semaphorins and subsequent remodeling of the
CC cytoskeleton. Plays a role in axon guidance, invasive growth and cell
CC migration. Class 3 semaphorins bind to a complex composed of a
CC neuropilin and a plexin. The plexin modulates the affinity of the
CC complex for specific semaphorins, and its cytoplasmic domain is
CC required for the activation of down-stream signaling events in the
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts directly with NRP1 and NRP2. Interacts with FARP2,
CC RND1 and KDR/VEGFR2. Binding of SEMA3A leads to dissociation of FARP2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in fetal brain, lung, liver and kidney.
CC {ECO:0000269|PubMed:8570614}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AC011199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X87832; CAB57274.1; -; mRNA.
DR EMBL; AK128612; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33847.2; -.
DR RefSeq; NP_115618.3; NM_032242.3.
DR AlphaFoldDB; Q9UIW2; -.
DR SMR; Q9UIW2; -.
DR BioGRID; 111375; 163.
DR CORUM; Q9UIW2; -.
DR IntAct; Q9UIW2; 15.
DR MINT; Q9UIW2; -.
DR STRING; 9606.ENSP00000377061; -.
DR GlyGen; Q9UIW2; 8 sites.
DR iPTMnet; Q9UIW2; -.
DR MetOSite; Q9UIW2; -.
DR PhosphoSitePlus; Q9UIW2; -.
DR SwissPalm; Q9UIW2; -.
DR BioMuta; PLXNA1; -.
DR DMDM; 313104202; -.
DR EPD; Q9UIW2; -.
DR jPOST; Q9UIW2; -.
DR MassIVE; Q9UIW2; -.
DR MaxQB; Q9UIW2; -.
DR PaxDb; Q9UIW2; -.
DR PeptideAtlas; Q9UIW2; -.
DR PRIDE; Q9UIW2; -.
DR ProteomicsDB; 84573; -.
DR ABCD; Q9UIW2; 2 sequenced antibodies.
DR Antibodypedia; 2368; 185 antibodies from 27 providers.
DR DNASU; 5361; -.
DR Ensembl; ENST00000393409.3; ENSP00000377061.2; ENSG00000114554.12.
DR GeneID; 5361; -.
DR KEGG; hsa:5361; -.
DR MANE-Select; ENST00000393409.3; ENSP00000377061.2; NM_032242.4; NP_115618.3.
DR UCSC; uc003ejg.3; human.
DR CTD; 5361; -.
DR DisGeNET; 5361; -.
DR GeneCards; PLXNA1; -.
DR HGNC; HGNC:9099; PLXNA1.
DR HPA; ENSG00000114554; Low tissue specificity.
DR MIM; 601055; gene.
DR neXtProt; NX_Q9UIW2; -.
DR OpenTargets; ENSG00000114554; -.
DR VEuPathDB; HostDB:ENSG00000114554; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; Q9UIW2; -.
DR OMA; WCVSERR; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q9UIW2; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; Q9UIW2; -.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q9UIW2; -.
DR SIGNOR; Q9UIW2; -.
DR BioGRID-ORCS; 5361; 17 hits in 1092 CRISPR screens.
DR ChiTaRS; PLXNA1; human.
DR GeneWiki; Plexin_A1; -.
DR GenomeRNAi; 5361; -.
DR Pharos; Q9UIW2; Tbio.
DR PRO; PR:Q9UIW2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UIW2; protein.
DR Bgee; ENSG00000114554; Expressed in middle temporal gyrus and 189 other tissues.
DR Genevisible; Q9UIW2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR GO; GO:0021628; P:olfactory nerve formation; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR CDD; cd11271; Sema_plexin_A1; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042744; Plexin-A1_Sema.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1896
FT /note="Plexin-A1"
FT /id="PRO_0000232745"
FT TOPO_DOM 27..1244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1266..1896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..512
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 864..959
FT /note="IPT/TIG 1"
FT DOMAIN 961..1045
FT /note="IPT/TIG 2"
FT DOMAIN 1048..1147
FT /note="IPT/TIG 3"
FT DOMAIN 1150..1236
FT /note="IPT/TIG 4"
FT COILED 1264..1317
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 130..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 286..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 302..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 376..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 515..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 521..563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 524..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 535..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 598..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 46
FT /note="A -> G (in Ref. 2; CAB57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> L (in Ref. 2; CAB57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="S -> N (in Ref. 2; CAB57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="F -> S (in Ref. 2; CAB57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="C -> R (in Ref. 2; CAB57274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1896 AA; 211067 MW; 76E5C9C0710C7FC1 CRC64;
MPLPPRSLQV LLLLLLLLLL LPGMWAEAGL PRAGGGSQPP FRTFSASDWG LTHLVVHEQT
GEVYVGAVNR IYKLSGNLTL LRAHVTGPVE DNEKCYPPPS VQSCPHGLGS TDNVNKLLLL
DYAANRLLAC GSASQGICQF LRLDDLFKLG EPHHRKEHYL SSVQEAGSMA GVLIAGPPGQ
GQAKLFVGTP IDGKSEYFPT LSSRRLMANE EDADMFGFVY QDEFVSSQLK IPSDTLSKFP
AFDIYYVYSF RSEQFVYYLT LQLDTQLTSP DAAGEHFFTS KIVRLCVDDP KFYSYVEFPI
GCEQAGVEYR LVQDAYLSRP GRALAHQLGL AEDEDVLFTV FAQGQKNRVK PPKESALCLF
TLRAIKEKIK ERIQSCYRGE GKLSLPWLLN KELGCINSPL QIDDDFCGQD FNQPLGGTVT
IEGTPLFVDK DDGLTAVAAY DYRGRTVVFA GTRSGRIRKI LVDLSNPGGR PALAYESVVA
QEGSPILRDL VLSPNHQYLY AMTEKQVTRV PVESCVQYTS CELCLGSRDP HCGWCVLHSI
CSRRDACERA DEPQRFAADL LQCVQLTVQP RNVSVTMSQV PLVLQAWNVP DLSAGVNCSF
EDFTESESVL EDGRIHCRSP SAREVAPITR GQGDQRVVKL YLKSKETGKK FASVDFVFYN
CSVHQSCLSC VNGSFPCHWC KYRHVCTHNV ADCAFLEGRV NVSEDCPQIL PSTQIYVPVG
VVKPITLAAR NLPQPQSGQR GYECLFHIPG SPARVTALRF NSSSLQCQNS SYSYEGNDVS
DLPVNLSVVW NGNFVIDNPQ NIQAHLYKCP ALRESCGLCL KADPRFECGW CVAERRCSLR
HHCAADTPAS WMHARHGSSR CTDPKILKLS PETGPRQGGT RLTITGENLG LRFEDVRLGV
RVGKVLCSPV ESEYISAEQI VCEIGDASSV RAHDALVEVC VRDCSPHYRA LSPKRFTFVT
PTFYRVSPSR GPLSGGTWIG IEGSHLNAGS DVAVSVGGRP CSFSWRNSRE IRCLTPPGQS
PGSAPIIINI NRAQLTNPEV KYNYTEDPTI LRIDPEWSIN SGGTLLTVTG TNLATVREPR
IRAKYGGIER ENGCLVYNDT TMVCRAPSVA NPVRSPPELG ERPDELGFVM DNVRSLLVLN
STSFLYYPDP VLEPLSPTGL LELKPSSPLI LKGRNLLPPA PGNSRLNYTV LIGSTPCTLT
VSETQLLCEA PNLTGQHKVT VRAGGFEFSP GTLQVYSDSL LTLPAIVGIG GGGGLLLLVI
VAVLIAYKRK SRDADRTLKR LQLQMDNLES RVALECKEAF AELQTDIHEL TNDLDGAGIP
FLDYRTYAMR VLFPGIEDHP VLKEMEVQAN VEKSLTLFGQ LLTKKHFLLT FIRTLEAQRS
FSMRDRGNVA SLIMTALQGE MEYATGVLKQ LLSDLIEKNL ESKNHPKLLL RRTESVAEKM
LTNWFTFLLY KFLKECAGEP LFMLYCAIKQ QMEKGPIDAI TGEARYSLSE DKLIRQQIDY
KTLTLNCVNP ENENAPEVPV KGLDCDTVTQ AKEKLLDAAY KGVPYSQRPK AADMDLEWRQ
GRMARIILQD EDVTTKIDND WKRLNTLAHY QVTDGSSVAL VPKQTSAYNI SNSSTFTKSL
SRYESMLRTA SSPDSLRSRT PMITPDLESG TKLWHLVKNH DHLDQREGDR GSKMVSEIYL
TRLLATKGTL QKFVDDLFET IFSTAHRGSA LPLAIKYMFD FLDEQADKHQ IHDADVRHTW
KSNCLPLRFW VNVIKNPQFV FDIHKNSITD ACLSVVAQTF MDSCSTSEHK LGKDSPSNKL
LYAKDIPNYK SWVERYYADI AKMPAISDQD MSAYLAEQSR LHLSQFNSMS ALHEIYSYIT
KYKDEILAAL EKDEQARRQR LRSKLEQVVD TMALSS
