ID   SPTN5_HUMAN             Reviewed;        3674 AA.
AC   Q9NRC6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Spectrin beta chain, non-erythrocytic 5;
DE   AltName: Full=Beta-V spectrin;
GN   Name=SPTBN5; Synonyms=BSPECV, HUBSPECV, HUSPECV;
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].
RC   TISSUE=Cerebellum, Retina, and Spinal cord;
RX   PubMed=10764729; DOI=10.1074/jbc.c000159200;
RA   Stabach P.R., Morrow J.S.;
RT   "Identification and characterization of beta V spectrin, a mammalian
RT   ortholog of Drosophila beta H spectrin.";
RL   J. Biol. Chem. 275:21385-21395(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [3]
RP   INTERACTION WITH TRPC4.
RX   PubMed=18048348; DOI=10.1074/jbc.m709729200;
RA   Odell A.F., Van Helden D.F., Scott J.L.;
RT   "The spectrin cytoskeleton influences the surface expression and activation
RT   of human transient receptor potential channel 4 channels.";
RL   J. Biol. Chem. 283:4395-4407(2008).
CC   -!- SUBUNIT: Probably associates with an alpha chain. Interacts (via C-
CC       terminus) with TRPC4. {ECO:0000269|PubMed:18048348}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Detected
CC       prominently in the outer segments of photoreceptor rods and cones and
CC       in the basolateral membrane and cytosol of gastric epithelial cells.
CC   -!- TISSUE SPECIFICITY: Expressed at very low levels in many tissues, with
CC       strongest expression in cerebellum, spinal cord, stomach, pituitary
CC       gland, liver, pancreas, salivary gland, kidney, bladder, and heart.
CC   -!- SIMILARITY: Belongs to the spectrin family. {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; AF233523; AAF65317.1; -; mRNA.
DR   EMBL; AC020659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS61599.1; -.
DR   RefSeq; NP_057726.4; NM_016642.3.
DR   SMR; Q9NRC6; -.
DR   BioGRID; 119479; 14.
DR   IntAct; Q9NRC6; 7.
DR   STRING; 9606.ENSP00000317790; -.
DR   iPTMnet; Q9NRC6; -.
DR   PhosphoSitePlus; Q9NRC6; -.
DR   BioMuta; SPTBN5; -.
DR   DMDM; 17369320; -.
DR   EPD; Q9NRC6; -.
DR   jPOST; Q9NRC6; -.
DR   MassIVE; Q9NRC6; -.
DR   PaxDb; 9606-ENSP00000317790; -.
DR   PeptideAtlas; Q9NRC6; -.
DR   ProteomicsDB; 82333; -.
DR   Antibodypedia; 57995; 72 antibodies from 15 providers.
DR   DNASU; 51332; -.
DR   Ensembl; ENST00000320955.8; ENSP00000317790.6; ENSG00000137877.10.
DR   GeneID; 51332; -.
DR   KEGG; hsa:51332; -.
DR   MANE-Select; ENST00000320955.8; ENSP00000317790.6; NM_016642.4; NP_057726.4.
DR   UCSC; uc001zos.5; human.
DR   AGR; HGNC:15680; -.
DR   CTD; 51332; -.
DR   DisGeNET; 51332; -.
DR   GeneCards; SPTBN5; -.
DR   HGNC; HGNC:15680; SPTBN5.
DR   HPA; ENSG00000137877; Group enriched (brain, retina).
DR   MIM; 605916; gene.
DR   neXtProt; NX_Q9NRC6; -.
DR   OpenTargets; ENSG00000137877; -.
DR   PharmGKB; PA38020; -.
DR   VEuPathDB; HostDB:ENSG00000137877; -.
DR   eggNOG; KOG0517; Eukaryota.
DR   GeneTree; ENSGT00940000161549; -.
DR   HOGENOM; CLU_000146_3_1_1; -.
DR   InParanoid; Q9NRC6; -.
DR   OMA; WANEMHA; -.
DR   OrthoDB; 2872403at2759; -.
DR   PhylomeDB; Q9NRC6; -.
DR   TreeFam; TF313446; -.
DR   PathwayCommons; Q9NRC6; -.
DR   Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   SignaLink; Q9NRC6; -.
DR   BioGRID-ORCS; 51332; 18 hits in 1117 CRISPR screens.
DR   ChiTaRS; SPTBN5; human.
DR   GeneWiki; SPTBN5; -.
DR   GenomeRNAi; 51332; -.
DR   Pharos; Q9NRC6; Tbio.
DR   PRO; PR:Q9NRC6; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NRC6; Protein.
DR   Bgee; ENSG00000137877; Expressed in sural nerve and 103 other cell types or tissues.
DR   GO; GO:0045179; C:apical cortex; IEA:Ensembl.
DR   GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR   GO; GO:0097381; C:photoreceptor disc membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008091; C:spectrin; NAS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0034452; F:dynactin binding; IDA:MGI.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR   GO; GO:0032029; F:myosin tail binding; IDA:MGI.
DR   GO; GO:0002046; F:opsin binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IDA:MGI.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR   GO; GO:0007041; P:lysosomal transport; IMP:MGI.
DR   CDD; cd21247; CH_SPTBN5_rpt1; 1.
DR   CDD; cd21249; CH_SPTBN5_rpt2; 1.
DR   CDD; cd00176; SPEC; 16.
DR   Gene3D; 1.20.58.60; -; 22.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 27.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 30.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 23.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q9NRC6; HS.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome;
KW   Repeat.
FT   CHAIN           1..3674
FT                   /note="Spectrin beta chain, non-erythrocytic 5"
FT                   /id="PRO_0000073466"
FT   DOMAIN          54..159
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          177..282
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          307..416
FT                   /note="Spectrin 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          428..529
FT                   /note="Spectrin 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          642..742
FT                   /note="Spectrin 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          747..810
FT                   /note="Spectrin 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          900..996
FT                   /note="Spectrin 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1103..1206
FT                   /note="Spectrin 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1209..1311
FT                   /note="Spectrin 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1315..1417
FT                   /note="Spectrin 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1521..1624
FT                   /note="Spectrin 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1628..1727
FT                   /note="Spectrin 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1731..1835
FT                   /note="Spectrin 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1842..1940
FT                   /note="Spectrin 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1944..2046
FT                   /note="Spectrin 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2052..2146
FT                   /note="Spectrin 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2150..2253
FT                   /note="Spectrin 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2256..2361
FT                   /note="Spectrin 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2366..2467
FT                   /note="Spectrin 17"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2471..2574
FT                   /note="Spectrin 18"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2577..2680
FT                   /note="Spectrin 19"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2683..2784
FT                   /note="Spectrin 20"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2791..2890
FT                   /note="Spectrin 21"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2894..2997
FT                   /note="Spectrin 22"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3000..3103
FT                   /note="Spectrin 23"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3106..3209
FT                   /note="Spectrin 24"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3213..3311
FT                   /note="Spectrin 25"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3318..3415
FT                   /note="Spectrin 26"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3422..3488
FT                   /note="Spectrin 27"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3533..3641
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..279
FT                   /note="Actin-binding"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1441..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1453..1467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         1345
FT                   /note="R -> H (in dbSNP:rs2290559)"
FT                   /id="VAR_022050"
FT   VARIANT         1367
FT                   /note="R -> T (in dbSNP:rs2290558)"
FT                   /id="VAR_024395"
FT   VARIANT         2862
FT                   /note="Q -> R (in dbSNP:rs1456235)"
FT                   /id="VAR_024396"
FT   VARIANT         3275
FT                   /note="A -> G (in dbSNP:rs1197660)"
FT                   /id="VAR_024397"
FT   CONFLICT        433
FT                   /note="H -> R (in Ref. 1; AAF65317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1035
FT                   /note="C -> R (in Ref. 1; AAF65317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1053
FT                   /note="H -> Y (in Ref. 1; AAF65317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3564
FT                   /note="N -> T (in Ref. 1; AAF65317)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3674 AA;  416750 MW;  83D1F94ADE670E13 CRC64;
     MAGQPHSPRE LLGAAGHRSR RPSTELRVPP SPSLTMDSQY ETGHIRKLQA RHMQMQEKTF
     TKWINNVFQC GQAGIKIRNL YTELADGIHL LRLLELISGE ALPPPSRGRL RVHFLENSSR
     ALAFLRAKVP VPLIGPENIV DGDQTLILGL IWVIILRFQI SHISLDKEEF GASAALLSTK
     EALLVWCQRK TASYTNVNIT DFSRSWSDGL GFNALIHAHR PDLLDYGSLR PDRPLHNLAF
     AFLVAEQELG IAQLLDPEDV AAAQPDERSI MTYVSLYYHY CSRLHQGQTV QRRLTKILLQ
     LQETELLQTQ YEQLVADLLR WIAEKQMQLE ARDFPDSLPA MRQLLAAFTI FRTQEKPPRL
     QQRGAAEALL FRLQTALQAQ NRRPFLPHEG LGLAELSQCW AGLEWAEAAR SQALQQRLLQ
     LQRLETLARR FQHKAALRES FLKDAEQVLD QARAPPASLA TVEAAVQRLG MLEAGILPQE
     GRFQALAEIA DILRQEQYHS WADVARRQEE VTVRWQRLLQ HLQGQRKQVA DMQAVLSLLQ
     EVEAASHQLE ELQEPARSTA CGQQLAEVVE LLQRHDLLEA QVSAHGAHVS HLAQQTAELD
     SSLGTSVEVL QAKARTLAQL QQSLVALVRA RRALLEQTLQ RAEFLRNCEE EEAWLKECGQ
     RVGNAALGRD LSQIAGALQK HKALEAEVHR HQAVCVDLVR RGRDLSARRP PTQPDPGERA
     EAVQGGWQLL QTRVVGRGAR LQTALLVLQY FADAAEAASW LRERRSSLER ASCGQDQAAA
     ETLLRRHVRL ERVLRAFAAE LRRLEEQGRA ASARASLFTV NSALSPPGES LRNPGPWSEA
     SCHPGPGDAW KMALPAEPDP DFDPNTILQT QDHLSQDYES LRALAQLRRA RLEEAMALFG
     FCSSCGELQL WLEKQTVLLQ RVQPQADTLE VMQLKYENFL TALAVGKGLW AEVSSSAEQL
     RQRYPGNSTQ IQRQQEELSQ RWGQLEALKR EKAVQLAHSV EVCSFLQECG PTQVQLRDVL
     LQLEALQPGS SEDTCHALQL AQKKTLVLER RVHFLQSVVV KVEEPGYAES QPLQGQVETL
     QGLLKQVQEQ VAQRARRQAE TQARQSFLQE SQQLLLWAES VQAQLRSKEV SVDVASAQRL
     LREHQDLLEE IHLWQERLQQ LDAQSQPMAA LDCPDSQEVP NTLRVLGQQG QELKVLWEQR
     QQWLQEGLEL QKFGREVDGF TATCANHQAW LHLDNLGEDV REALSLLQQH REFGRLLSTL
     GPRAEALRAH GEKLVQSQHP AAHTVREQLQ SIQAQWTRLQ GRSEQRRRQL LASLQLQEWK
     QDVAELMQWM EEKGLMAAHE PSGARRNILQ TLKRHEAAES ELLATRRHVE ALQQVGRELL
     SRRPCGQEDI QTRLQGLRSK WEALNRKMTE RGDELQQAGQ QEQLLRQLQD AKEQLEQLEG
     ALQSSETGQD LRSSQRLQKR HQQLESESRT LAAKMAALAS MAHGMAASPA ILEETQKHLR
     RLELLQGHLA IRGLQLQASV ELHQFCHLSN MELSWVAEHM PHGSPTSYTE CLNGAQSLHR
     KHKELQVEVK AHQGQVQRVL SSGRSLAASG HPQAQHIVEQ CQELEGHWAE LERACEARAQ
     CLQQAVTFQQ YFLDVSELEG WVEEKRPLVS SRDYGRDEAA TLRLINKHQA LQEELAIYWS
     SMEELDQTAQ TLTGPEVPEQ QRVVQERLRE QLRALQELAA TRDRELEGTL RLHEFLREAE
     DLQGWLASQK QAAKGGESLG EDPEHALHLC TKFAKFQHQV EMGSQRVAAC RLLAESLLER
     GHSAGPMVRQ RQQDLQTAWS ELWELTQARG HALRDTETTL RVHRDLLEVL TQVQEKATSL
     PNNVARDLCG LEAQLRSHQG LERELVGTER QLQELLETAG RVQKLCPGPQ AHAVQQRQQA
     VTQAWAVLQR RMEQRRAQLE RARLLARFRT AVRDYASWAA RVRQDLQVEE SSQEPSSGPL
     KLSAHQWLRA ELEAREKLWQ QATQLGQQAL LAAGTPTKEV QEELRALQDQ RDQVYQTWAR
     KQERLQAEQQ EQLFLRECGR LEEILAAQEV SLKTSALGSS VEEVEQLIRK HEVFLKVLTA
     QDKKEAALRE RLKTLRRPRV RDRLPILLQR RMRVKELAES RGHALHASLL MASFTQAATQ
     AEDWIQAWAQ QLKEPVPPGD LRDKLKPLLK HQAFEAEVQA HEEVMTSVAK KGEALLAQSH
     PRAGEVSQRL QGLRKHWEDL RQAMALRGQE LEDRRNFLEF LQRVDLAEAW IQEKEVKMNV
     GDLGQDLEHC LQLRRRLREF RGNSAGDTVG DACIRSISDL SLQLKNRDPE EVKIICQRRS
     QLNNRWASFH GNLLRYQQQL EGALEIHVLS RELDNVTKRI QEKEALIQAL DCGKDLESVQ
     RLLRKHEELE REVHPIQAQV ESLEREVGRL CQRSPEAAHG LRHRQQEVAE SWWQLRSRAQ
     KRREALDALH QAQKLQAMLQ ELLVSAQRLR AQMDTSPAPR SPVEARRMLE EHQECKAELD
     SWTDSISLAR STGQQLLTAG HPFSSDIRQV LAGLEQELSS LEGAWQEHQL QLQQALELQL
     FLSSVEKMER WLCSKEDSLA SEGLWDPLAP MEPLLWKHKM LEWDLEVQAG KISALEATAR
     GLHQGGHPEA QSALGRCQAM LLRKEALFRQ AGTRRHRLEE LRQLQAFLQD SQEVAAWLRE
     KNLVALEEGL LDTAMLPAQL QKQQNFQAEL DASMHQQQEL QREGQRLLQG GHPASEAIQE
     RLEELGALWG ELQDNSQKKV AKLQKACEAL RLRRSMEELE NWLEPIEVEL RAPTVGQALP
     GVGELLGTQR ELEAAVDKKA RQAEALLGQA QAFVREGHCL AQDVEEQARR LLQRFKSLRE
     PLQERRTALE ARSLLLKFFR DADEEMAWVQ EKLPLAAAQD YGQSLSAVRH LQEQHQNLES
     EMSSHEALTR VVLGTGYKLV QAGHFAAHEV AARVQQLEKA MAHLRAEAAR RRLLLQQAQE
     AQQFLTELLE AGSWLAERGH VLDSEDMGHS AEATQALLRR LEATKRDLEA FSPRIERLQQ
     TAALLESRKN PESPKVLAQL QAVREAHAEL LRRAEARGHG LQEQLQLHQL ERETLLLDAW
     LTTKAATAES QDYGQDLEGV KVLEEKFDAF RKEVQSLGQA KVYALRKLAG TLERGAPRRY
     PHIQAQRSRI EAAWERLDQA IKARTENLAA AHEVHSFQQA AAELQGRMQE KTALMKGEDG
     GHSLSSVRTL QQQHRRLERE LEAMEKEVAR LQTEACRLGQ LHPAAPGGLA KVQEAWATLQ
     AKAQERGQWL AQAAQGHAFL GRCQELLAWA QERQELASSE ELAEDVAGAE QLLGQHEELG
     QEIRECRLQA QDLRQEGQQL VDNSHFMSAE VTECLQELEG RLQELEEAWA LRWQRCAESW
     GLQKLRQRLE QAEAWLACWE GLLLKPDYGH SVSDVELLLH RHQDLEKLLA AQEEKFAQMQ
     KTEMEQELLL QPQELKPGRA GSSLTSFQWR PSGHQGLGAQ LAETRDPQDA KGTPTMEGSL
     EFKQHLLPGG RQPSSSSWDS CRGNLQGSSL SLFLDERMAA EKVASIALLD LTGARCERLR
     GRHGRKHTFS LRLTSGAEIL FAAPSEEQAE SWWRALGSTA AQSLSPKLKA KPVSSLNECT
     TKDARPGCLL RSDP
//