APBA1_MOUSE
ID APBA1_MOUSE Reviewed; 842 AA.
AC B2RUJ5; Q3UH49; Q8BMF2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 1;
DE AltName: Full=Adapter protein X11alpha;
DE AltName: Full=Neuron-specific X11 protein;
DE AltName: Full=Neuronal Munc18-1-interacting protein 1;
DE Short=Mint-1;
GN Name=Apba1 {ECO:0000312|MGI:MGI:1860297};
GN Synonyms=Mint1 {ECO:0000312|MGI:MGI:1860297},
GN mLin-10 {ECO:0000303|PubMed:10846156}, X11 {ECO:0000312|MGI:MGI:1860297};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP PROTEIN SEQUENCE OF 498-525 (ISOFORM 3), INTERACTION WITH RAB6A,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23737971; DOI=10.1371/journal.pone.0064149;
RA Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G.,
RA Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K.,
RA Kins S., Goud B., Barnekow A.;
RT "A new Mint1 isoform, but not the conventional Mint1, interacts with the
RT small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [6]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH CASK AND LIN7, AND INTERACTION
RP WITH KIF17.
RX PubMed=10846156; DOI=10.1126/science.288.5472.1796;
RA Setou M., Nakagawa T., Seog D.-H., Hirokawa N.;
RT "Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-
RT containing vesicle transport.";
RL Science 288:1796-1802(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-246; SER-250;
RP SER-252; SER-267; SER-284; THR-309; SER-317; SER-372; THR-375; SER-406;
RP SER-408 AND SER-413, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Putative function in synaptic vesicle exocytosis by binding
CC to Munc18-1, an essential component of the synaptic vesicle exocytotic
CC machinery. May modulate processing of the amyloid-beta precursor
CC protein (APP) and hence formation of AAP-beta (By similarity).
CC Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the
CC motor protein KIF17 to transport vesicles containing N-methyl-D-
CC aspartate (NMDA) receptor subunit NR2B along microtubules
CC (PubMed:10846156). {ECO:0000250, ECO:0000269|PubMed:10846156}.
CC -!- SUBUNIT: Part of a multimeric complex containing Munc18-1 and syntaxin-
CC 1. Component of the brain-specific heterotrimeric complex (LIN-10-LIN-
CC 2-LIN-7 complex) composed of at least APBA1, CASK, and LIN7, which
CC associates with the motor protein KIF17 to transport vesicles along
CC microtubules (PubMed:10846156). Within the complex, interacts (via PDZ
CC domain) with the motor protein KIF17; the interaction is direct and is
CC required for association of KIF17 with the cargo that is to be
CC transported (PubMed:10846156). Binds to the cytoplasmic domain of
CC amyloid protein (APP) (By similarity). Interacts (via PDZ 1 and 2
CC domains) with FSPB (By similarity). Isoform 3 interacts (via its
CC truncated PID domain) with active, GTP-bound RAB6A. Also interacts with
CC GTP-bound RAB6B (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10846156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B2RUJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2RUJ5-2; Sequence=VSP_043763, VSP_043764;
CC Name=3; Synonyms=Mint1_826;
CC IsoId=B2RUJ5-3; Sequence=VSP_053519;
CC -!- TISSUE SPECIFICITY: Isoform 3 is expressed in brain.
CC {ECO:0000269|PubMed:23737971}.
CC -!- DOMAIN: Composed of an N-terminal domain that binds Munc18-1 and LIN-
CC 2/CASK, a middle phosphotyrosine-binding domain (PID/PTB) that mediates
CC binding with the cytoplasmic domain of the amyloid-beta precursor
CC protein, and two C-terminal PDZ domains thought to attach proteins to
CC the plasma membrane. {ECO:0000250}.
CC -!- DOMAIN: The autoinhibitory helix linker occludes the APP binding site.
CC {ECO:0000250}.
CC -!- DOMAIN: The PID domain, truncated by 11 amino acids, as observed in
CC isoform 3, but not full-length, mediates the interaction with RAB6A.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: This isoform interacts with RAB6 GTPases.
CC {ECO:0000305}.
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DR EMBL; AK032261; BAC27784.1; -; mRNA.
DR EMBL; AK147583; BAE28008.1; -; mRNA.
DR EMBL; AC134830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC148021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466534; EDL41607.1; -; Genomic_DNA.
DR EMBL; CH466534; EDL41608.1; -; Genomic_DNA.
DR EMBL; BC141181; AAI41182.1; -; mRNA.
DR CCDS; CCDS50407.1; -. [B2RUJ5-1]
DR RefSeq; NP_796008.2; NM_177034.3. [B2RUJ5-1]
DR RefSeq; XP_006527202.1; XM_006527139.3. [B2RUJ5-1]
DR RefSeq; XP_006527203.1; XM_006527140.3. [B2RUJ5-3]
DR PDB; 6LNM; X-ray; 2.40 A; B/D/F=351-394.
DR PDBsum; 6LNM; -.
DR AlphaFoldDB; B2RUJ5; -.
DR BMRB; B2RUJ5; -.
DR SMR; B2RUJ5; -.
DR BioGRID; 235626; 10.
DR CORUM; B2RUJ5; -.
DR ELM; B2RUJ5; -.
DR IntAct; B2RUJ5; 2.
DR STRING; 10090.ENSMUSP00000025830; -.
DR iPTMnet; B2RUJ5; -.
DR PhosphoSitePlus; B2RUJ5; -.
DR jPOST; B2RUJ5; -.
DR PaxDb; B2RUJ5; -.
DR PeptideAtlas; B2RUJ5; -.
DR PRIDE; B2RUJ5; -.
DR ProteomicsDB; 296411; -. [B2RUJ5-1]
DR ProteomicsDB; 296412; -. [B2RUJ5-2]
DR ProteomicsDB; 296413; -. [B2RUJ5-3]
DR Antibodypedia; 12360; 218 antibodies from 38 providers.
DR DNASU; 319924; -.
DR Ensembl; ENSMUST00000025830; ENSMUSP00000025830; ENSMUSG00000024897. [B2RUJ5-1]
DR Ensembl; ENSMUST00000237688; ENSMUSP00000157770; ENSMUSG00000024897. [B2RUJ5-2]
DR GeneID; 319924; -.
DR KEGG; mmu:319924; -.
DR UCSC; uc008hai.1; mouse. [B2RUJ5-1]
DR CTD; 320; -.
DR MGI; MGI:1860297; Apba1.
DR VEuPathDB; HostDB:ENSMUSG00000024897; -.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000156820; -.
DR HOGENOM; CLU_013563_1_0_1; -.
DR InParanoid; B2RUJ5; -.
DR OMA; DCEDQRP; -.
DR OrthoDB; 436779at2759; -.
DR PhylomeDB; B2RUJ5; -.
DR TreeFam; TF315245; -.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 319924; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Apba1; mouse.
DR PRO; PR:B2RUJ5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; B2RUJ5; protein.
DR Bgee; ENSMUSG00000024897; Expressed in habenula and 157 other tissues.
DR Genevisible; B2RUJ5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0014047; P:glutamate secretion; IGI:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IPI:MGI.
DR GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR030530; Apba1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR12345:SF14; PTHR12345:SF14; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Golgi apparatus; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..842
FT /note="Amyloid-beta A4 precursor protein-binding family A
FT member 1"
FT /id="PRO_0000417501"
FT DOMAIN 460..648
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 661..746
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 752..828
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..648
FT /note="Autoinhibitory helix linker"
FT /evidence="ECO:0000250"
FT COMPBIAS 104..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35430"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35430"
FT VAR_SEQ 1..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_043763"
FT VAR_SEQ 391..405
FT /note="SPTRDCDDQRPVDGD -> MENFWMYQFESHEEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_043764"
FT VAR_SEQ 500..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053519"
FT CONFLICT 142
FT /note="V -> A (in Ref. 4; AAI41182)"
FT /evidence="ECO:0000305"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:6LNM"
SQ SEQUENCE 842 AA; 92909 MW; E00B754EDCF1B1D4 CRC64;
MNHLEGSAEV EVADEAPGGE VNESVEADLE HPEVVEGQQP SPSPPPPAGH EPEDHRGHPA
PPPPPPPQEE EEEERGECLA RSASTESGFH NHTDTAEGDV LAAARDGYEA ERAQDADDES
AYAVQYRPEA EEYTEQAEAE HVEAAQRRAL PNHLHFHSLE HEEAMNAAYS GYVYTHRLFH
RAEDEPYAEP YADYGGLQEH VYEEIGDAPE LEARDGLRLY ERERDEAAAY RQEALGARLH
HYDERSDGES DSPEKEAEFA PYPRMDSYEQ EEDIDQIVAE VKQSMSSQSL DKAAEDMPEA
EQDLERAPTP GGGHPDSPGL PAPAGQQQRV VGTPGGSEVG QRYSKEKRDA ISLAIKDIKE
AIEEVKTRTI RSPYTPDEPK EPIWVMRQDI SPTRDCDDQR PVDGDSPSPG SSSPLGAESS
SIPLHPGDPT EASTNKESRK SLASFPTYVE VPGPCDPEDL IDGIIFAANY LGSTQLLSDK
TPSKNVRMMQ AQEAVSRIKT AQKLAKSRKK APEGESQPMT EVDLFISTQR IKVLNADTQE
PMMDHPLRTI SYIADIGNIV VLMARRRMPR SNSQENVEAS HPSQDGKRQY KMICHVFESE
DAQLIAQSIG QAFSVAYQEF LRANGINPED LSQKEYSDLL NTQDMYNDDL IHFSKSENCK
DVFIEKQKGE ILGVVIVESG WGSILPTVII ANMMHGGPAE KSGKLNIGDQ IMSINGTSLV
GLPLSTCQSI IKGLKNQSRV KLNIVRCPPV TTVLIRRPDL RYQLGFSVQN GIICSLMRGG
IAERGGVRVG HRIIEINGQS VVATPHEKIV HILSNAVGEI HMKTMPAAMY RLLTAQEQPV
YI
