PCD16_RAT
ID PCD16_RAT Reviewed; 3291 AA.
AC D4ACX8;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protocadherin-16;
DE AltName: Full=Protein dachsous homolog 1;
DE Flags: Precursor;
GN Name=Dchs1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions
CC in neuroprogenitor cell proliferation and differentiation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterophilic interaction with FAT4; this interaction affects
CC their respective protein levels. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and
CC DCHS1 accumulated at the cell-cell boundaries located apical to the
CC adherens junction.
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DR EMBL; AABR06007653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101014.2; NM_001107544.2.
DR RefSeq; XP_006230004.1; XM_006229942.2.
DR SMR; D4ACX8; -.
DR STRING; 10116.ENSRNOP00000040147; -.
DR GlyGen; D4ACX8; 4 sites.
DR iPTMnet; D4ACX8; -.
DR PhosphoSitePlus; D4ACX8; -.
DR jPOST; D4ACX8; -.
DR PaxDb; D4ACX8; -.
DR PeptideAtlas; D4ACX8; -.
DR PRIDE; D4ACX8; -.
DR Ensembl; ENSRNOT00000042865; ENSRNOP00000040147; ENSRNOG00000031643.
DR GeneID; 308912; -.
DR KEGG; rno:308912; -.
DR UCSC; RGD:1309878; rat.
DR CTD; 8642; -.
DR RGD; 1309878; Dchs1.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161822; -.
DR HOGENOM; CLU_000265_2_0_1; -.
DR InParanoid; D4ACX8; -.
DR OMA; RVMAYDP; -.
DR OrthoDB; 34489at2759; -.
DR TreeFam; TF316403; -.
DR PRO; PR:D4ACX8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000031643; Expressed in heart and 17 other tissues.
DR Genevisible; D4ACX8; RN.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; ISO:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0072137; P:condensed mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0003192; P:mitral valve formation; ISO:RGD.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISO:RGD.
DR GO; GO:0072006; P:nephron development; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0036342; P:post-anal tail morphogenesis; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 9.
DR Pfam; PF00028; Cadherin; 23.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 27.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 18.
DR PROSITE; PS50268; CADHERIN_2; 27.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..3291
FT /note="Protocadherin-16"
FT /id="PRO_0000429046"
FT TOPO_DOM 36..2933
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2934..2954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2955..3291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..137
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..249
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 250..356
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 369..466
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 476..572
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 573..679
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 680..784
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 785..888
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 889..994
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 995..1105
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1100..1205
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1218..1317
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1326..1429
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1430..1539
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1539..1642
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1643..1744
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1745..1848
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1849..1953
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1976..2061
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2062..2164
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2165..2270
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2270..2369
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2370..2475
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2476..2595
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2596..2699
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2700..2806
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2807..2926
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 951..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2978..3033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3051..3080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3226..3291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3232..3255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3048
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVD3"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3291 AA; 345981 MW; B2C15E55E42CE503 CRC64;
MQEELSVALS CPGMKSLGTL LPLLVLLGTT VPGIRGQAGS LDLQIDEEQP AGTLIGDISA
GLPPGTAPPP MYFISAQEGS GVGTDLDIDE HSGVVCTARV LDRERRDRYR FTAVTPDGAT
VEVTVRVADI NDHAPAFPQA RAALQIPEHT ALGTRYPLEP AHDADAGRLG TQGYALSGDG
AGETFRLETR PGPGGAPVPE LVIAGELDRE NRSHYMLQLE AYDGGSPPRR AQALLDVTLL
DINDHAPAFN QSRYHAVVSE SLAPGSPVLQ VFASDADAGA NGAVTYEINR RQSEGDGPFS
IDAHTGFLKL ERPLDFEQRR VHELVVQARD GGAHPELGSA FVTVHVRDAN DNQPSMTVIF
LSADGSPRVS EAAPPGQLVA RISVSDPDDG DFAHVNVSLE GGEGHFALST QDSVIYLVCV
ARRLDREERD VYNLRVTATD SGSPPLRAEA AFVLHVTDVN DNAPAFDRQL YRPEPLPEVA
LPGSFVVRVT ARDPDQGTNG QVTYSLAPGT HTHWFSIDPT SGIITTAATL DYELEPQPQL
IVVATDGGLP PLVSSATVSV ALQDVNDNEP QFQRTFYNAS LPEGTQPGTC FLQVTATDAD
SGPFGLLSYS LGAGLGASGS PPFRIDAHSG EVCTTRILDR DQGPSSFDFT VTAIDGGGLK
SMVYVKVFVA DENDNPPQFY PREYAASLSA QSTPGTAVLR VHAHDPDQGP HGRLSYHILA
GNSPPLFALD AHSGLLTVAW PLGRRANSVV QLEIGAQDGG GLQAEPIARV NISIVPGTPT
PPIFEQLQYV FSVPEDVAPG TSVGVVQAHN PPGRLGPVTL TLSGGDPRGL FSLDSASGLL
KTLRPLDREL LGPVLELEVR AGSGTPPVFS AARIRVLLDD VNDNSPAFPA PEDTVLLPQN
TAPGTPVYTL RALDPDSGAN SRVTFSLLAG GDGLFTVDPT TGHVRLMGPL GPPGGPPHEL
EVEAQDGGSP PRTSHFRLRV VIQDLGIHGL APRFDSPTYR VDLPSGTTTG TQILQVQAQA
PDGSPVTYHL AADGASNPFG LESQSGWLWV RAALDRESQE LYTLKVMAVS GSKAELGQQT
GTATVRVVIL NQNDHSPRLS EEPTFLAVAE NQPPGTSVGR VFATDKDSGP NGRLTYSLQQ
LSEDSKAFRI HPQTGEVTTL QTLDREQQSS FQLLVQVQDA GSPPRSATGT VHVAVLDLND
NSPTFLQASG AAGGGLPIQV PDRVPPGTLV TTLQAKDPDE GENGTILYTL TGSGSELFSL
HPHTGELHTA ASLIRAERPH YVLTLSAHDQ GSPPRSASLQ LLVQVLPSTR MVESPDLVEA
DSAATVPVVL TVTAAEGLRP GSLLGSVAPQ EPASMGVLTY TLVGGADPEG TFALDSASGR
LYLARVLDFE SGPAWRALTV RAEGPGGAGA RLMRVQVRVQ DENEHAPAFA RDPLALALPE
NPEPGATLYT FRASDADGPG PNSDVRYRLL RQEPPVPALR LDARTGALSA PRGLDRETTP
ALLLIVEATD RPANASRRKA TRVSARVFVT DENDNAPVFA SPSRMRLPED QPPGPAALHV
VARDPDLGEA ARVSYRLAAG GDGHFRLHAT TGALSVVRPL DREQRAEHVL TVVASDHGSP
PRSSTQLLTV SVVDVNDEAP AFPQQEYNVI LRENSPPGTS LLTLKATDPD LGANGQVTYG
GVSGESFSLD PNSGVLTTLR ALDREEQEEI NLTVYARDRG LPPLLTHITV RVTVEDENDH
SPTFGNTHLS LEVPEGQDPQ TLTTLRASDP DGGLNGQLQY RILGGDPSGA FALDLTSGEF
GTTRPLDREV EPAFQLQIEA RDGGQPALSA TLLVTVTVLD ANDHAPAFPV PSYSVEVPED
APVGTLLLQL QAHDPDEGDN GRVMYYLGAG TAGAFLLEPT SGELSTATAL DREHCASYAF
SVTAVDGAAA GPLSTTVPIT VTVRDVNDHA PAFPTSPLRL RLPRPGPSLN KPTLALATLR
AEDRDAGANA SILYRLAGTP PPGTTVDSYT GEIRVARSPA ALGPRDRVLF IVATDLGRPA
RSATGVVIVG IQGEPERGPR FPRANNEAVL RENAPPGTPV ISPKAVHSGG SNGPITYSIL
SGNERGIFSI QPSTGTITVQ SAEGLDFETN PRLRLVLQAE SGGAFAFSVL TLTLQDANDN
APRFLQPHYV AFLPESRPLE GPLLQVEADD LDQGSGGQIS YSLAASQPAR GLFHVDPATG
TITTTAILDR EIWAETRLVL MATDRGSPAL VGSATLTVMV IDTNDNRPTI PQPWELRVSE
DALLGSEIAQ VTGNDVDSGP VLWYVLSPSG PQDPFSIGRY GGRVSLTGPL DFEQCDHYHL
QLLAHDGPHE GHANLTVLVE DVNDNVPIFS QSLYQVMMLE HTPPGSAILS VSATDRDSGA
NGHISYHLAS PAEGFSVDTN NGTLFTTVGA MALGHEGPGV VDVVLEARDH GAPGRSAQAT
VHVQLKDQND HAPSFTLPHY RVAVSEDLPP GSTLLTLEAI DADGSRSHAT VDYSIISGNR
GRVFQLEPRL AEVGDGVGPG PQALGCLVLL EPLDFESLTQ YNLTVTAADR GQPPRSSAVP
VTVTVLDVND NPPVFTRASY RVTVPEDMPV GAELLHVEAS DADPGPHGLV HFTLSSGDPL
GLFELDENSG ALRLAHPLDC ETQAQHQLVV QAADPAGTHF ALVPVTVEVQ DVNDHGPAFP
LSLLSTSLAE NQPPGTLVTT LHAMDGDAGT FGRLRYTLLE AVPGPEGREA FSLNSSTGEL
RARVPFDYEH TGSFRLLVGA ADAGNLSASV TVSVLITGED EYDPVFLAPS FHFQVPEGAQ
RGHSLGHVQA TDEDGGADGL VLYSLATSSP YFGINQTTGA LYLRVDSRAP GSGTATSGGG
GRTRREAPRE LRLEVVARGP LPGSRSATVP VTVDITHTAL GLAPDLNLLL VGAVAASLGV
VVVLALAALV LGLVRARSRK AEAAPGPMSQ TAPIASSSLQ KLGREPPSPP PSEHLYHQTL
PSYGGPGAGG PYPRGGSLDP SHSSGRGSAE AAEDDEIRMI NEFPRVASVA SSLAARGPDS
GIQQDADGLS DTSCEPPAPD TWYKGRKAGL LLPGAGATLY REEGPPATAT AFLGGCGLSP
APTGDYGFPA DGKPCVAGAL TAIVAGEEEL RGSYNWDYLL SWCPQFQPLA SVFTEIARLK
DEARPCPPAP RIDPPPLITA VAHPGAKSVP PKPASTAATR AIFPPASHRS PISHEGSLSS
AAMSPSFSPS LSPLAARSPV VSPFGVAQGP SASALSTESG LEPPDDTELR I
