APLP1_MOUSE
ID APLP1_MOUSE Reviewed; 654 AA.
AC Q03157; A0A0R4IZZ1; Q3U311; Q8VC38;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Amyloid beta precursor like protein 1 {ECO:0000250|UniProtKB:P51693};
DE AltName: Full=Amyloid beta (A4) precursor-like protein 1 {ECO:0000312|MGI:MGI:88046};
DE AltName: Full=Amyloid-like protein 1 {ECO:0000250|UniProtKB:P51693};
DE Short=APLP {ECO:0000250|UniProtKB:P51693};
DE Short=APLP-1;
DE Contains:
DE RecName: Full=C30;
DE Flags: Precursor;
GN Name=Aplp1;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=1279693; DOI=10.1073/pnas.89.22.10758;
RA Wasco W., Bupp K., Magendantz M., Gusella J.F., Tanzi R.E., Solomon F.;
RT "Identification of a mouse brain cDNA that encodes a protein related to the
RT Alzheimer disease-associated amyloid beta protein precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10758-10762(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 COLLAGEN-BINDING.
RX PubMed=8576160; DOI=10.1074/jbc.271.3.1613;
RA Beher D., Hesse L., Masters C.L., Multhaup G.;
RT "Regulation of amyloid protein precursor (APP) binding to collagen and
RT mapping of the binding sites on APP and collagen type I.";
RL J. Biol. Chem. 271:1613-1620(1996).
RN [6]
RP INTERACTION WITH DAB1.
RX PubMed=10460257; DOI=10.1523/jneurosci.19-17-07507.1999;
RA Homayouni R., Rice D.S., Sheldon M., Curran T.;
RT "Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like
RT protein 1.";
RL J. Neurosci. 19:7507-7515(1999).
RN [7]
RP INTERACTION WITH MAPK8IP1.
RX PubMed=11517249; DOI=10.1523/jneurosci.21-17-06597.2001;
RA Matsuda S., Yasukawa T., Homma Y., Ito Y., Niikura T., Hiraki T., Hirai S.,
RA Ohno S., Kita Y., Kawasumi M., Kouyama K., Yamamoto T., Kyriakis J.M.,
RA Nishimoto I.;
RT "C-jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1
RT scaffolds Alzheimer's amyloid precursor protein with JNK.";
RL J. Neurosci. 21:6597-6607(2001).
RN [8]
RP INTERACTION WITH DAB2.
RX PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
RA Morris S.M., Cooper J.A.;
RT "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts
RT with AP-2.";
RL Traffic 2:111-123(2001).
RN [9]
RP PROTEOLYTIC PROCESSING BY GAMMA SECRETASE, INTERACTION WITH APBB1, AND
RP MUTAGENESIS OF TYR-642.
RX PubMed=12228233; DOI=10.1074/jbc.m208110200;
RA Scheinfeld M.H., Ghersi E., Laky K., Fowlkes B.J., D'Adamio L.;
RT "Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-
RT secretase regulates transcription.";
RL J. Biol. Chem. 277:44195-44201(2002).
RN [10]
RP INTERACTION WITH DAB1.
RX PubMed=12826668; DOI=10.1074/jbc.m304384200;
RA Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J.,
RA Rock C.O., Curran T., Park H.W.;
RT "Crystal structures of the Dab homology domains of mouse disabled 1 and
RT 2.";
RL J. Biol. Chem. 278:36572-36581(2003).
RN [11]
RP INTERACTION WITH CPEB1.
RX PubMed=16314516; DOI=10.1128/mcb.25.24.10930-10939.2005;
RA Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
RT "Amyloid precursor proteins anchor CPEB to membranes and promote
RT polyadenylation-induced translation.";
RL Mol. Cell. Biol. 25:10930-10939(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: May play a role in postsynaptic function. The C-terminal
CC gamma-secretase processed fragment, ALID1, activates transcription
CC activation through APBB1 (Fe65) binding. Couples to JIP signal
CC transduction through C-terminal binding. May interact with cellular G-
CC protein signaling pathways. Can regulate neurite outgrowth through
CC binding to components of the extracellular matrix such as heparin and
CC collagen I.
CC -!- FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of neuronal
CC apoptosis. {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. Heparin binding promotes
CC homodimerization. Binds, via its C-terminus, to the PID domain of
CC several cytoplasmic proteins, including APBB and APBA family members,
CC MAPK8IP1 and DAB1 (By similarity). Binding to Dab1 inhibits its serine
CC phosphorylation. Interacts with CPEB1. Interacts (via NPXY motif) with
CC DAB2 (via PID domain); the interaction is impaired by tyrosine
CC phosphorylation of the NPXY motif. Interacts (via NPXY motif) with
CC DAB1. {ECO:0000250, ECO:0000269|PubMed:10460257,
CC ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11517249,
CC ECO:0000269|PubMed:12228233, ECO:0000269|PubMed:12826668,
CC ECO:0000269|PubMed:16314516}.
CC -!- INTERACTION:
CC Q03157; P12023: App; NbExp=4; IntAct=EBI-399929, EBI-78814;
CC Q03157; P97318: Dab1; NbExp=4; IntAct=EBI-399929, EBI-81680;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [C30]: Cytoplasm. Note=C-terminally processed in
CC the Golgi complex.
CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated
CC proteins is required for the specific binding of the PID domain.
CC However, additional amino acids either N- or C-terminal to the NPXY
CC motif are often required for complete interaction. The NPXY site is
CC also involved in clathrin-mediated endocytosis.
CC -!- PTM: Proteolytically cleaved by caspases during neuronal apoptosis.
CC Cleaved, in vitro, at Asp-624 by caspase-3 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated.
CC -!- MISCELLANEOUS: Binds zinc and copper in the extracellular domain. Zinc-
CC binding increases heparin binding. No Cu(2+) reducing activity with
CC copper-binding.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01217}.
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; L04538; AAA37247.1; -; mRNA.
DR EMBL; AK154992; BAE32979.1; -; mRNA.
DR EMBL; JH584274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021877; AAH21877.1; -; mRNA.
DR CCDS; CCDS21092.1; -.
DR PIR; A46362; A46362.
DR RefSeq; NP_031493.2; NM_007467.3.
DR AlphaFoldDB; Q03157; -.
DR SMR; Q03157; -.
DR BioGRID; 198153; 10.
DR IntAct; Q03157; 9.
DR MINT; Q03157; -.
DR STRING; 10090.ENSMUSP00000006828; -.
DR GlyGen; Q03157; 2 sites.
DR iPTMnet; Q03157; -.
DR PhosphoSitePlus; Q03157; -.
DR CPTAC; non-CPTAC-3635; -.
DR MaxQB; Q03157; -.
DR PaxDb; Q03157; -.
DR PeptideAtlas; Q03157; -.
DR PRIDE; Q03157; -.
DR ProteomicsDB; 283160; -.
DR ProteomicsDB; 332404; -.
DR Antibodypedia; 16162; 266 antibodies from 28 providers.
DR DNASU; 11803; -.
DR Ensembl; ENSMUST00000006828; ENSMUSP00000006828; ENSMUSG00000006651.
DR GeneID; 11803; -.
DR KEGG; mmu:11803; -.
DR UCSC; uc009gek.2; mouse.
DR CTD; 333; -.
DR MGI; MGI:88046; Aplp1.
DR VEuPathDB; HostDB:ENSMUSG00000006651; -.
DR eggNOG; KOG3540; Eukaryota.
DR GeneTree; ENSGT00530000063252; -.
DR InParanoid; Q03157; -.
DR OMA; CKSYVYW; -.
DR OrthoDB; 953529at2759; -.
DR PhylomeDB; Q03157; -.
DR TreeFam; TF317274; -.
DR BioGRID-ORCS; 11803; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Aplp1; mouse.
DR PRO; PR:Q03157; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q03157; protein.
DR Bgee; ENSMUSG00000006651; Expressed in nucleus accumbens and 192 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:MGI.
DR GO; GO:0031695; F:alpha-2B adrenergic receptor binding; ISO:MGI.
DR GO; GO:0031696; F:alpha-2C adrenergic receptor binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071874; P:cellular response to norepinephrine stimulus; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IGI:MGI.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:MGI.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; IDA:MGI.
DR Gene3D; 1.20.120.770; -; 1.
DR Gene3D; 3.30.1490.140; -; 1.
DR Gene3D; 3.90.570.10; -; 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR PANTHER; PTHR23103; PTHR23103; 1.
DR Pfam; PF10515; APP_amyloid; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF109843; SSF109843; 1.
DR SUPFAM; SSF56491; SSF56491; 1.
DR SUPFAM; SSF89811; SSF89811; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
DR PROSITE; PS00320; APP_INTRA; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell adhesion; Cell membrane; Copper; Cytoplasm; Disulfide bond;
KW Endocytosis; Glycoprotein; Heparin-binding; Membrane; Metal-binding;
KW Neurodegeneration; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..654
FT /note="Amyloid beta precursor like protein 1"
FT /id="PRO_0000000205"
FT PEPTIDE 625..654
FT /note="C30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000206"
FT TOPO_DOM 39..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..212
FT /note="E1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DOMAIN 297..488
FT /note="E2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT REGION 50..146
FT /note="GFLD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 154..212
FT /note="CuBD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 214..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..346
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 414..445
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 446..463
FT /note="Collagen-binding"
FT /evidence="ECO:0000250"
FT REGION 497..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..652
FT /note="Interaction with DAB1"
FT REGION 640..654
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000269|PubMed:11247302"
FT MOTIF 608..619
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250"
FT MOTIF 644..647
FT /note="NPXY motif; contains endocytosis signal"
FT COMPBIAS 529..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 565
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT SITE 624..625
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 95..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 120..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 156..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 167..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 181..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT MUTAGEN 642
FT /note="Y->G: Reduced binding of APBB1."
FT /evidence="ECO:0000269|PubMed:12228233"
FT CONFLICT 19
FT /note="Missing (in Ref. 1; AAA37247)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="H -> P (in Ref. 2; BAE32979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 72848 MW; D72A3065D8D95F68 CRC64;
MGPTSPAARG QGRRWRPPPL PLLLPLSLLL LRAQLAVGNL AVGSPSAAEA PGSAQVAGLC
GRLTLHRDLR TGRWEPDPQR SRRCLLDPQR VLEYCRQMYP ELHIARVEQA AQAIPMERWC
GGTRSGRCAH PHHEVVPFHC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA
CSSQGLILHG SGMLLPCGSD RFRGVEYVCC PPPATPNPSG MAAGDPSTRS WPLGGRAEGG
EDEEEVESFP QPVDDYFVEP PQAEEEEEEE EERAPPPSSH TPVMVSRVTP TPRPTDGVDV
YFGMPGEIGE HEGFLRAKMD LEERRMRQIN EVMREWAMAD SQSKNLPKAD RQALNEHFQS
ILQTLEEQVS GERQRLVETH ATRVIALIND QRRAALEGFL AALQGDPPQA ERVLMALRRY
LRAEQKEQRH TLRHYQHVAA VDPEKAQQMR FQVQTHLQVI EERMNQSLGL LDQNPHLAQE
LRPQIQELLL AEHLGPSELD ASVPGSSSED KGSLQPPESK DDPPVTLPKG STDQESSSSG
REKLTPLEQY EQKVNASAPR GFPFHSSDIQ RDELAPSGTG VSREALSGLL IMGAGGGSLI
VLSLLLLRKK KPYGTISHGV VEVDPMLTLE EQQLRELQRH GYENPTYRFL EERP
