ID BASP1_HUMAN Reviewed; 227 AA. AC P80723; B4DJA8; D3DTD5; O43596; Q5U0S0; Q9BWA5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Brain acid soluble protein 1; DE AltName: Full=22 kDa neuronal tissue-enriched acidic protein; DE AltName: Full=Neuronal axonal membrane protein NAP-22; GN Name=BASP1; Synonyms=NAP22; 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). RX PubMed=9749536; RA Park S., Kim Y.-I., Kim B., Seong C., Oh Y., Baek K., Yoon J.; RT "Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa RT neuronal tissue-enriched acidic protein) homologs."; RL Mol. Cells 8:471-477(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [6] RP PROTEIN SEQUENCE OF 2-227, MYRISTOYLATION AT GLY-2, AND MASS SPECTROMETRY. RC TISSUE=Brain; RX PubMed=9310187; DOI=10.1016/s0300-9084(97)80032-6; RA Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A., RA Plekhanov A.Y.U., Zakharov V.V.; RT "The BASP1 family of myristoylated proteins abundant in axonal termini. RT Primary structure analysis and physico-chemical properties."; RL Biochimie 79:373-384(1997). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164; SER-170; RP SER-172; SER-176; THR-196 AND SER-205, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; SER-164; SER-205 AND RP SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25255805; DOI=10.1038/ncomms5919; RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated proteomes RT in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-163, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-84 AND LYS-97, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- INTERACTION: CC P80723; Q99732: LITAF; NbExp=3; IntAct=EBI-358583, EBI-725647; CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, CC growth cone. Note=Associated with the membranes of growth cones that CC form the tips of elongating axons. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P80723-1; Sequence=Displayed; CC Name=2; CC IsoId=P80723-2; Sequence=VSP_037994; CC -!- TISSUE SPECIFICITY: Brain. CC -!- MASS SPECTROMETRY: Mass=22780; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:9310187}; CC -!- SIMILARITY: Belongs to the BASP1 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; AF039656; AAC67374.1; -; mRNA. DR EMBL; BT019340; AAV38147.1; -; mRNA. DR EMBL; BT019341; AAV38148.1; -; mRNA. DR EMBL; AK295995; BAG58770.1; -; mRNA. DR EMBL; CH471102; EAX08012.1; -; Genomic_DNA. DR EMBL; CH471102; EAX08013.1; -; Genomic_DNA. DR EMBL; BC000518; AAH00518.1; -; mRNA. DR CCDS; CCDS3888.1; -. [P80723-1] DR RefSeq; NP_001258535.1; NM_001271606.1. [P80723-1] DR RefSeq; NP_006308.3; NM_006317.4. [P80723-1] DR AlphaFoldDB; P80723; -. DR BMRB; P80723; -. DR BioGRID; 115680; 307. DR IntAct; P80723; 90. DR MINT; P80723; -. DR STRING; 9606.ENSP00000319281; -. DR TCDB; 1.A.71.1.1; the brain acid-soluble protein channel (basp1 channel) family. DR GlyCosmos; P80723; 2 sites, 1 glycan. DR GlyGen; P80723; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P80723; -. DR PhosphoSitePlus; P80723; -. DR SwissPalm; P80723; -. DR BioMuta; BASP1; -. DR DMDM; 6686256; -. DR CPTAC; CPTAC-31; -. DR CPTAC; CPTAC-32; -. DR EPD; P80723; -. DR jPOST; P80723; -. DR MassIVE; P80723; -. DR MaxQB; P80723; -. DR PaxDb; 9606-ENSP00000319281; -. DR PeptideAtlas; P80723; -. DR ProteomicsDB; 57688; -. [P80723-1] DR ProteomicsDB; 57689; -. [P80723-2] DR Pumba; P80723; -. DR TopDownProteomics; P80723-1; -. [P80723-1] DR TopDownProteomics; P80723-2; -. [P80723-2] DR Antibodypedia; 54132; 186 antibodies from 26 providers. DR DNASU; 10409; -. DR Ensembl; ENST00000322611.4; ENSP00000319281.3; ENSG00000176788.9. [P80723-1] DR Ensembl; ENST00000616743.1; ENSP00000482066.1; ENSG00000176788.9. [P80723-1] DR GeneID; 10409; -. DR KEGG; hsa:10409; -. DR MANE-Select; ENST00000322611.4; ENSP00000319281.3; NM_006317.5; NP_006308.3. DR UCSC; uc003jfx.5; human. [P80723-1] DR AGR; HGNC:957; -. DR CTD; 10409; -. DR DisGeNET; 10409; -. DR GeneCards; BASP1; -. DR HGNC; HGNC:957; BASP1. DR HPA; ENSG00000176788; Tissue enhanced (brain, epididymis). DR MIM; 605940; gene. DR neXtProt; NX_P80723; -. DR OpenTargets; ENSG00000176788; -. DR PharmGKB; PA25261; -. DR VEuPathDB; HostDB:ENSG00000176788; -. DR eggNOG; ENOG502RXJZ; Eukaryota. DR GeneTree; ENSGT00730000111450; -. DR HOGENOM; CLU_093511_0_0_1; -. DR InParanoid; P80723; -. DR OMA; PMFDEPN; -. DR PathwayCommons; P80723; -. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR SignaLink; P80723; -. DR BioGRID-ORCS; 10409; 30 hits in 1159 CRISPR screens. DR ChiTaRS; BASP1; human. DR GeneWiki; BASP1; -. DR GenomeRNAi; 10409; -. DR Pharos; P80723; Tbio. DR PRO; PR:P80723; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P80723; Protein. DR Bgee; ENSG00000176788; Expressed in orbitofrontal cortex and 205 other cell types or tissues. DR ExpressionAtlas; P80723; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0000785; C:chromatin; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB. DR GO; GO:0060539; P:diaphragm development; ISS:UniProtKB. DR GO; GO:0008406; P:gonad development; ISS:UniProtKB. DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB. DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0072112; P:podocyte differentiation; ISS:UniProtKB. DR GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB. DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB. DR DisProt; DP00930; -. DR InterPro; IPR008408; BASP1. DR PANTHER; PTHR23212; BRAIN ACID SOLUBLE PROTEIN 1; 1. DR PANTHER; PTHR23212:SF0; BRAIN ACID SOLUBLE PROTEIN 1; 1. DR Pfam; PF05466; BASP1; 1. DR Genevisible; P80723; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cell projection; KW Direct protein sequencing; Isopeptide bond; Lipoprotein; Membrane; KW Myristate; Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:9310187" FT CHAIN 2..227 FT /note="Brain acid soluble protein 1" FT /id="PRO_0000142895" FT REGION 1..227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..102 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 165..201 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 31 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 36 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XV3" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91XV3" FT MOD_RES 196 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:9310187" FT CROSSLNK 25 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 84 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 97 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 163 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 88..141 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037994" FT VARIANT 76 FT /note="A -> V (in dbSNP:rs3733748)" FT /id="VAR_048396" FT CONFLICT 45 FT /note="A -> P (in Ref. 1; AAC67374)" FT /evidence="ECO:0000305" FT CONFLICT 114..115 FT /note="AA -> LR (in Ref. 1; AAC67374)" FT /evidence="ECO:0000305" FT CONFLICT 128..132 FT /note="APAES -> GPRPR (in Ref. 1; AAC67374)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="E -> G (in Ref. 5; AAH00518)" FT /evidence="ECO:0000305" SQ SEQUENCE 227 AA; 22693 MW; 56FFFCEA441062AB CRC64; MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ DAEGKAEEKE GEKDAAAAKE EAPKAEPEKT EGAAEAKAEP PKAPEQEQAA PGPAAGGEAP KAAEAAAAPA ESAAPAAGEE PSKEEGEPKK TEAPAAPAAQ ETKSDGAPAS DSKPGSSEAA PSSKETPAAT EAPSSTPKAQ GPAASAEEPK PVEAPAANSD QTVTVKE //