BASP1_RAT
ID BASP1_RAT Reviewed; 220 AA.
AC Q05175;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8390468; DOI=10.1016/s0021-9258(18)86914-9;
RA Maekawa S., Maekawa M., Hattori S., Nakamura S.;
RT "Purification and molecular cloning of a novel acidic calmodulin binding
RT protein from rat brain.";
RL J. Biol. Chem. 268:13703-13709(1993).
RN [2]
RP PROTEIN SEQUENCE OF 11-18; 39-52; 91-157 AND 179-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
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 [4]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=8193160; DOI=10.1016/0167-4781(94)90113-9;
RA Maekawa S., Matsuura Y., Nakaruma S.;
RT "Expression and myristoylation of NAP-22 using a baculovirus transfer
RT vector system.";
RL Biochim. Biophys. Acta 1218:119-122(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-127 AND SER-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Brain.
CC -!- SIMILARITY: Belongs to the BASP1 family. {ECO:0000305}.
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DR EMBL; D14441; BAA03333.1; -; mRNA.
DR PIR; A46597; A46597.
DR RefSeq; NP_071636.1; NM_022300.1.
DR AlphaFoldDB; Q05175; -.
DR BioGRID; 248987; 8.
DR ELM; Q05175; -.
DR IntAct; Q05175; 1.
DR MINT; Q05175; -.
DR iPTMnet; Q05175; -.
DR PhosphoSitePlus; Q05175; -.
DR SwissPalm; Q05175; -.
DR jPOST; Q05175; -.
DR PeptideAtlas; Q05175; -.
DR PRIDE; Q05175; -.
DR GeneID; 64160; -.
DR KEGG; rno:64160; -.
DR UCSC; RGD:621491; rat.
DR CTD; 10409; -.
DR RGD; 621491; Basp1.
DR InParanoid; Q05175; -.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q05175; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0072112; P:podocyte differentiation; ISO:RGD.
DR InterPro; IPR008408; BASP1.
DR PANTHER; PTHR23212; PTHR23212; 1.
DR Pfam; PF05466; BASP1; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; 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:8193160"
FT CHAIN 2..220
FT /note="Brain acid soluble protein 1"
FT /id="PRO_0000142897"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XV3"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XV3"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:8193160"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
SQ SEQUENCE 220 AA; 21790 MW; ED7C9401EDB89147 CRC64;
MGSKLSKKKK GYNVNDEKAK DKDKKAEGAG TEEEGTQKES EPQAAADATE VKESAEEKPK
DAADGEAKAE EKEADKAAAK EEAPKAEPEK SEGAAEEQPE PAPAPEQEAA APGPAAGGEA
PKAGEASAES TGAADGAPQE EGEAKKTEAP AAGPEAKSDA APAASDSKPS TEPAPSSKET
PAASEAPSSA AKAPAPAAPA AEPQAEAPVA SSEQSVAVKE
