ID   RIMB1_HUMAN             Reviewed;        1857 AA.
AC   O95153; O75111; Q8N5W3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Peripheral-type benzodiazepine receptor-associated protein 1;
DE            Short=PRAX-1;
DE   AltName: Full=Peripheral benzodiazepine receptor-interacting protein;
DE            Short=PBR-IP;
DE   AltName: Full=RIMS-binding protein 1;
DE            Short=RIM-BP1;
DE   AltName: Full=TSPO-associated protein 1 {ECO:0000312|HGNC:HGNC:16831};
GN   Name=TSPOAP1 {ECO:0000312|HGNC:HGNC:16831};
GN   Synonyms=BZRAP1, KIAA0612, RBP1, RIMBP1;
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), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH TSPO.
RC   TISSUE=Brain;
RX   PubMed=9915832; DOI=10.1074/jbc.274.5.2938;
RA   Galiegue S., Jbilo O., Combes T., Bribes E., Carayon P., Le Fur G.,
RA   Casellas P.;
RT   "Cloning and characterization of PRAX-1. A new protein that specifically
RT   interacts with the peripheral benzodiazepine receptor.";
RL   J. Biol. Chem. 274:2938-2952(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-817;
RP   ARG-851; LEU-1118; PRO-1140 AND ARG-1728.
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 MRNA] OF 1737-1857 (ISOFORM 3).
RC   TISSUE=Brain;
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   [4]
RP   VARIANT ARG-652.
RX   PubMed=23375655; DOI=10.1016/j.ajhg.2013.01.003;
RA   Parry D.A., Poulter J.A., Logan C.V., Brookes S.J., Jafri H.,
RA   Ferguson C.H., Anwari B.M., Rashid Y., Zhao H., Johnson C.A.,
RA   Inglehearn C.F., Mighell A.J.;
RT   "Identification of mutations in SLC24A4, encoding a potassium-dependent
RT   sodium/calcium exchanger, as a cause of amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 92:307-312(2013).
RN   [5]
RP   VARIANT DYT22AO SER-1808, CHARACTERIZATION OF VARIANT DYT22AO SER-1808,
RP   INVOLVEMENT IN DYT22AO, INVOLVEMENT IN DYT22JO, INTERACTION WITH CACNA1A,
RP   AND FUNCTION.
RX   PubMed=33539324; DOI=10.1172/jci140625;
RA   Mencacci N.E., Brockmann M.M., Dai J., Pajusalu S., Atasu B., Campos J.,
RA   Pino G., Gonzalez-Latapi P., Patzke C., Schwake M., Tucci A., Pittman A.,
RA   Simon-Sanchez J., Carvill G.L., Balint B., Wiethoff S., Warner T.T.,
RA   Papandreou A., Soo A., Rein R., Kadastik-Eerme L., Puusepp S., Reinson K.,
RA   Tomberg T., Hanagasi H., Gasser T., Bhatia K.P., Kurian M.A., Lohmann E.,
RA   Ounap K., Rosenmund C., Suedhof T.C., Wood N.W., Krainc D., Acuna C.;
RT   "Biallelic variants in TSPOAP1, encoding the active-zone protein RIMBP1,
RT   cause autosomal recessive dystonia.";
RL   J. Clin. Invest. 131:0-0(2021).
CC   -!- FUNCTION: Required for synaptic transmission regulation
CC       (PubMed:33539324). It probably controls the recruitement of voltage-
CC       gated calcium channels to the presynaptic membrane, and modulates
CC       neurotransmitter release. {ECO:0000269|PubMed:33539324}.
CC   -!- SUBUNIT: Interacts with RIMS1 and RIMS2 (By similarity). Interacts with
CC       TSPO. Interacts with CACNA1A (PubMed:33539324). {ECO:0000250,
CC       ECO:0000269|PubMed:33539324, ECO:0000269|PubMed:9915832}.
CC   -!- INTERACTION:
CC       O95153; Q9H013: ADAM19; NbExp=2; IntAct=EBI-5915931, EBI-8567699;
CC       O95153; O00555: CACNA1A; NbExp=2; IntAct=EBI-5915931, EBI-766279;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9915832}.
CC       Mitochondrion {ECO:0000269|PubMed:9915832}. Note=Preferentially
CC       expressed in the mitochondria in the presence of TSPO.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O95153-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95153-2; Sequence=VSP_009204;
CC       Name=3;
CC         IsoId=O95153-3; Sequence=VSP_009205;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain, pituitary gland
CC       and thymus in adults. In adult brain, highest expression found in
CC       temporal lobe and the putamen, followed by amygdala, caudate nucleus,
CC       cerebral cortex, occipital and frontal lobe. A high expression level is
CC       also observed in fetal tissues like brain, heart, kidney and thymus.
CC       {ECO:0000269|PubMed:9915832}.
CC   -!- DOMAIN: The SH3 and proline-rich domain is required for the interaction
CC       with TSPO and the second SH3 domain mediates binding to a proline-rich
CC       motif in RIMS1 and RIMS2. {ECO:0000250}.
CC   -!- DISEASE: Dystonia 22, adult-onset (DYT22AO) [MIM:620456]: A form of
CC       dystonia, a disorder defined by the presence of sustained involuntary
CC       muscle contraction, often leading to abnormal postures. DYT22AO is an
CC       autosomal recessive form characterized by focal dystonia or tremor and
CC       mild cognitive impairment. {ECO:0000269|PubMed:33539324}. Note=The
CC       disease may be caused by variants affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Dystonia 22, juvenile-onset (DYT22JO) [MIM:620453]: A form of
CC       dystonia, a disorder defined by the presence of sustained involuntary
CC       muscle contraction, often leading to abnormal postures. DYT22JO is an
CC       autosomal recessive form characterized by progressive, generalized
CC       dystonia associated with intellectual disability, cognitive decline,
CC       and cerebellar atrophy. {ECO:0000269|PubMed:33539324}. Note=The disease
CC       may be caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:9915832 demonstrated interaction with TSPO but later
CC       PubMed:12435798 demonstrated in the rat ortholog that is not associated
CC       with TSPO in the brain. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31587.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF039571; AAD11957.1; -; mRNA.
DR   EMBL; AB014512; BAA31587.2; ALT_INIT; mRNA.
DR   EMBL; BC031401; AAH31401.1; -; mRNA.
DR   CCDS; CCDS11605.1; -. [O95153-1]
DR   CCDS; CCDS45742.1; -. [O95153-2]
DR   PIR; T00391; T00391.
DR   RefSeq; NP_001248764.1; NM_001261835.1.
DR   RefSeq; NP_004749.2; NM_004758.3. [O95153-1]
DR   RefSeq; NP_077729.1; NM_024418.2. [O95153-2]
DR   RefSeq; XP_006722236.1; XM_006722173.2.
DR   AlphaFoldDB; O95153; -.
DR   SMR; O95153; -.
DR   BioGRID; 114680; 23.
DR   IntAct; O95153; 11.
DR   MINT; O95153; -.
DR   STRING; 9606.ENSP00000345824; -.
DR   BindingDB; O95153; -.
DR   ChEMBL; CHEMBL5169104; -.
DR   TCDB; 8.A.34.3.1; the endophilin (endophilin) family.
DR   CarbonylDB; O95153; -.
DR   iPTMnet; O95153; -.
DR   PhosphoSitePlus; O95153; -.
DR   BioMuta; TSPOAP1; -.
DR   EPD; O95153; -.
DR   jPOST; O95153; -.
DR   MassIVE; O95153; -.
DR   PaxDb; 9606-ENSP00000345824; -.
DR   PeptideAtlas; O95153; -.
DR   ProteomicsDB; 50666; -. [O95153-1]
DR   ProteomicsDB; 50667; -. [O95153-2]
DR   ProteomicsDB; 50668; -. [O95153-3]
DR   Antibodypedia; 18369; 28 antibodies from 12 providers.
DR   DNASU; 9256; -.
DR   Ensembl; ENST00000268893.10; ENSP00000268893.6; ENSG00000005379.17. [O95153-2]
DR   Ensembl; ENST00000343736.9; ENSP00000345824.4; ENSG00000005379.17. [O95153-1]
DR   GeneID; 9256; -.
DR   KEGG; hsa:9256; -.
DR   MANE-Select; ENST00000343736.9; ENSP00000345824.4; NM_004758.4; NP_004749.2.
DR   UCSC; uc002ivx.6; human. [O95153-1]
DR   AGR; HGNC:16831; -.
DR   CTD; 9256; -.
DR   DisGeNET; 9256; -.
DR   GeneCards; TSPOAP1; -.
DR   HGNC; HGNC:16831; TSPOAP1.
DR   HPA; ENSG00000005379; Tissue enhanced (brain).
DR   MalaCards; TSPOAP1; -.
DR   MIM; 610764; gene.
DR   MIM; 620453; phenotype.
DR   MIM; 620456; phenotype.
DR   neXtProt; NX_O95153; -.
DR   OpenTargets; ENSG00000005379; -.
DR   Orphanet; 101150; Autosomal recessive dopa-responsive dystonia.
DR   PharmGKB; PA128394545; -.
DR   VEuPathDB; HostDB:ENSG00000005379; -.
DR   eggNOG; KOG3632; Eukaryota.
DR   GeneTree; ENSGT00950000183203; -.
DR   HOGENOM; CLU_001979_1_0_1; -.
DR   InParanoid; O95153; -.
DR   OMA; VSAPMPR; -.
DR   OrthoDB; 5403222at2759; -.
DR   PhylomeDB; O95153; -.
DR   TreeFam; TF316230; -.
DR   PathwayCommons; O95153; -.
DR   Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-196108; Pregnenolone biosynthesis.
DR   Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   SignaLink; O95153; -.
DR   SIGNOR; O95153; -.
DR   BioGRID-ORCS; 9256; 15 hits in 1147 CRISPR screens.
DR   ChiTaRS; TSPOAP1; human.
DR   GenomeRNAi; 9256; -.
DR   Pharos; O95153; Tbio.
DR   PRO; PR:O95153; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O95153; Protein.
DR   Bgee; ENSG00000005379; Expressed in right uterine tube and 177 other cell types or tissues.
DR   ExpressionAtlas; O95153; baseline and differential.
DR   GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0030156; F:benzodiazepine receptor binding; IPI:UniProtKB.
DR   GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd12014; SH3_RIM-BP_1; 1.
DR   CDD; cd12012; SH3_RIM-BP_2; 1.
DR   CDD; cd12013; SH3_RIM-BP_3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035753; RIM-BP_SH3_2.
DR   InterPro; IPR035755; RIM-BP_SH3_3.
DR   InterPro; IPR040325; RIMBP1/2/3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14234:SF20; PERIPHERAL-TYPE BENZODIAZEPINE RECEPTOR-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF07653; SH3_2; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   Genevisible; O95153; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Disease variant; Dystonia;
KW   Intellectual disability; Mitochondrion; Reference proteome; Repeat;
KW   SH3 domain.
FT   CHAIN           1..1857
FT                   /note="Peripheral-type benzodiazepine receptor-associated
FT                   protein 1"
FT                   /id="PRO_0000221380"
FT   DOMAIN          653..720
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          791..882
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          884..976
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          981..1081
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1625..1693
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1764..1831
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1330..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1501..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1723..1761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1823..1857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1259..1275
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1411..1427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1554..1570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1842..1857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         191..250
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9734811"
FT                   /id="VSP_009204"
FT   VAR_SEQ         1849..1857
FT                   /note="RTRRRRVQC -> DWGCTTQGSPGPPGGPCTPSSGSAPRIERGEPQGRSEKV
FT                   WGFFSKGKQLLRRLGSGKKE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009205"
FT   VARIANT         514
FT                   /note="Q -> R (in dbSNP:rs2072145)"
FT                   /id="VAR_017446"
FT   VARIANT         586
FT                   /note="A -> T (in dbSNP:rs2072147)"
FT                   /id="VAR_017447"
FT   VARIANT         652
FT                   /note="G -> R (in dbSNP:rs373894175)"
FT                   /evidence="ECO:0000269|PubMed:23375655"
FT                   /id="VAR_070193"
FT   VARIANT         817
FT                   /note="Q -> R (in dbSNP:rs9913145)"
FT                   /evidence="ECO:0000269|PubMed:9734811"
FT                   /id="VAR_031662"
FT   VARIANT         851
FT                   /note="W -> R (in dbSNP:rs9905604)"
FT                   /evidence="ECO:0000269|PubMed:9734811"
FT                   /id="VAR_031663"
FT   VARIANT         1118
FT                   /note="H -> L (in dbSNP:rs3744099)"
FT                   /evidence="ECO:0000269|PubMed:9734811"
FT                   /id="VAR_017448"
FT   VARIANT         1140
FT                   /note="A -> P (in dbSNP:rs2680704)"
FT                   /evidence="ECO:0000269|PubMed:9734811"
FT                   /id="VAR_017449"
FT   VARIANT         1253
FT                   /note="R -> C (in dbSNP:rs3744101)"
FT                   /id="VAR_017450"
FT   VARIANT         1728
FT                   /note="H -> R (in dbSNP:rs11079346)"
FT                   /evidence="ECO:0000269|PubMed:9734811"
FT                   /id="VAR_031664"
FT   VARIANT         1808
FT                   /note="G -> S (in DYT22AO; likely pathogenic; abnormally
FT                   increased synaptic transmission when expressed in
FT                   RIMBPs-deficient autaptic neuronal cultures; increased
FT                   interaction with CACNA1A)"
FT                   /evidence="ECO:0000269|PubMed:33539324"
FT                   /id="VAR_088765"
FT   VARIANT         1830
FT                   /note="G -> E (in dbSNP:rs2301868)"
FT                   /id="VAR_017451"
FT   CONFLICT        1525
FT                   /note="G -> R (in Ref. 1; AAD11957)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1857 AA;  200051 MW;  594F850C95F9EE02 CRC64;
     MEQLTTLPRP GDPGAMEPWA LPTWHSWTPG RGGEPSSAAP SIADTPPAAL QLQELRSEES
     SKPKGDGSSR PVGGTDPEGA EACLPSLGQQ ASSSGPACQR PEDEEVEAFL KAKLNMSFGD
     RPNLELLRAL GELRQRCAIL KEENQMLRKS SFPETEEKVR RLKRKNAELA VIAKRLEERA
     RKLQETNLRV VSAPLPRPGT SLELCRKALA RQRARDLSET ASALLAKDKQ IAALQRECRE
     LQARLTLVGK EGPQWLHVRD FDRLLRESQR EVLRLQRQIA LRNQRETLPL PPSWPPGPAL
     QARAGAPAPG APGEATPQED ADNLPVILGE PEKEQRVQQL ESELSKKRKK CESLEQEARK
     KQRRCEELEL QLRQAQNENA RLVEENSRLS GRATEKEQVE WENAELRGQL LGVTQERDSA
     LRKSQGLQSK LESLEQVLKH MREVAQRRQQ LEVEHEQARL SLREKQEEVR RLQQAQAEAQ
     REHEGAVQLL ESTLDSMQAR VRELEEQCRS QTEQFSLLAQ ELQAFRLHPG PLDLLTSALD
     CGSLGDCPPP PCCCSIPQPC RGSGPKDLDL PPGSPGRCTP KSSEPAPATL TGVPRRTAKK
     AESLSNSSHS ESIHNSPKSC PTPEVDTASE VEELEADSVS LLPAAPEGSR GGARIQVFLA
     RYSYNPFEGP NENPEAELPL TAGEYIYIYG NMDEDGFFEG ELMDGRRGLV PSNFVERVSD
     DDLLTSLPPE LADLSHSSGP ELSFLSVGGG GSSSGGQSSV GRSQPRPEEE DAGDELSLSP
     SPEGLGEPPA VPYPRRLVVL KQLAHSVVLA WEPPPEQVEL HGFHICVNGE LRQALGPGAP
     PKAVLENLDL WAGPLHISVQ ALTSRGSSDP LRCCLAVGAR AGVVPSQLRV HRLTATSAEI
     TWVPGNSNLA HAIYLNGEEC PPASPSTYWA TFCHLRPGTP YQAQVEAQLP PQGPWEPGWE
     RLEQRAATLQ FTTLPAGPPD APLDVQIEPG PSPGILIISW LPVTIDAAGT SNGVRVTGYA
     IYADGQKIME VASPTAGSVL VELSQLQLLQ VCREVVVRTM SPHGESADSI PAPITPALAP
     ASLPARVSCP SPHPSPEARA PLASASPGPG DPSSPLQHPA PLGTQEPPGA PPASPSREMA
     KGSHEDPPAP CSQEEAGAAV LGTSEERTAS TSTLGEKDPG PAAPSLAKQE AEWTAGEACP
     ASSSTQGARA QQAPNTEMCQ GGDPGSGLRP RAEKEDTAEL GVHLVNSLVD HGRNSDLSDI
     QEEEEEEEEE EEEELGSRTC SFQKQVAGNS IRENGAKSQP DPFCETDSDE EILEQILELP
     LQQFCSKKLF SIPEEEEEEE EDEEEEKSGA GCSSRDPGPP EPALLGLGCD SGQPRRPGQC
     PLSPESSRAG DCLEDMPGLV GGSSRRRGGG SPEKPPSRRR PPDPREHCSR LLSNNGPQAS
     GRLGPTRERG GLPVIEGPRT GLEASGRGRL GPSRRCSRGR ALEPGLASCL SPKCLEISIE
     YDSEDEQEAG SGGISITSSC YPGDGEAWGT ATVGRPRGPP KANSGPKPYP RLPAWEKGEP
     ERRGRSATGR AKEPLSRATE TGEARGQDGS GRRGPQKRGV RVLRPSTAEL VPARSPSETL
     AYQHLPVRIF VALFDYDPVS MSPNPDAGEE ELPFREGQIL KVFGDKDADG FYQGEGGGRT
     GYIPCNMVAE VAVDSPAGRQ QLLQRGYLSP DILLEGSGNG PFVYSTAHTT GPPPKPRRSK
     KAESEGPAQP CPGPPKLVPS ADLKAPHSMV AAFDYNPQES SPNMDVEAEL PFRAGDVITV
     FGGMDDDGFY YGELNGQRGL VPSNFLEGPG PEAGGLDREP RTPQAESQRT RRRRVQC
//