SPTN2_RAT
ID SPTN2_RAT Reviewed; 2388 AA.
AC Q9QWN8; O88197; Q9ES68;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Spectrin beta chain, non-erythrocytic 2;
DE AltName: Full=Beta SpIII sigma 1;
DE AltName: Full=Beta-III spectrin;
DE AltName: Full=Glutamate transporter EAAT4-associated protein 41;
DE AltName: Full=SPNB-3;
DE AltName: Full=Spectrin-like protein GTRAP41;
GN Name=Sptbn2; Synonyms=Spnb3;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9675416; DOI=10.1016/s0169-328x(98)00068-0;
RA Ohara O., Ohara R., Yamakawa H., Nakajima D., Nakayama M.;
RT "Characterization of a new beta-spectrin gene which is predominantly
RT expressed in brain.";
RL Brain Res. Mol. Brain Res. 57:181-192(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9704016; DOI=10.1006/bbrc.1998.9067;
RA Sakaguchi G., Orita S., Naito A., Maeda M., Igarashi H., Sasaki T.,
RA Takai Y.;
RT "A novel brain-specific isoform of beta spectrin: isolation and its
RT interaction with Munc13.";
RL Biochem. Biophys. Res. Commun. 248:846-851(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11242047; DOI=10.1038/35065091;
RA Jackson M., Song W., Liu M.-Y., Jin L., Dykes-Hoberg M., Lin C.-L.G.,
RA Bowers W.J., Federoff H.J., Sternweis P.C., Rothstein J.D.;
RT "Modulation of the neuronal glutamate transporter EAAT4 by two interacting
RT proteins.";
RL Nature 410:89-93(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1574, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-31; SER-1073; SER-2169
RP AND SER-2199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- FUNCTION: Probably plays an important role in neuronal membrane
CC skeleton.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- TISSUE SPECIFICITY: Abundantly transcribed in the brain. Neurons are
CC the predominant cell-type to express the gene. Found abundantly in
CC Purkinje cells.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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DR EMBL; AB008551; BAA32699.1; -; mRNA.
DR EMBL; AB001347; BAA32473.1; -; mRNA.
DR EMBL; AF225960; AAG28596.1; -; mRNA.
DR PIR; JE0271; JE0271.
DR AlphaFoldDB; Q9QWN8; -.
DR BMRB; Q9QWN8; -.
DR SMR; Q9QWN8; -.
DR BioGRID; 247889; 6.
DR IntAct; Q9QWN8; 2.
DR MINT; Q9QWN8; -.
DR STRING; 10116.ENSRNOP00000026573; -.
DR iPTMnet; Q9QWN8; -.
DR PhosphoSitePlus; Q9QWN8; -.
DR jPOST; Q9QWN8; -.
DR PaxDb; Q9QWN8; -.
DR PRIDE; Q9QWN8; -.
DR UCSC; RGD:3751; rat.
DR RGD; 3751; Sptbn2.
DR eggNOG; KOG0517; Eukaryota.
DR InParanoid; Q9QWN8; -.
DR PhylomeDB; Q9QWN8; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR PRO; PR:Q9QWN8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; TAS:UniProtKB.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0033010; C:paranodal junction; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0099189; C:postsynaptic spectrin-associated cytoskeleton; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0008091; C:spectrin; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR GO; GO:0098918; F:structural constituent of synapse; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0099173; P:postsynapse organization; ISO:RGD.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; TAS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0016081; P:synaptic vesicle docking; TAS:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IPI:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00033; CH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15020"
FT CHAIN 2..2388
FT /note="Spectrin beta chain, non-erythrocytic 2"
FT /id="PRO_0000073464"
FT DOMAIN 57..161
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 176..281
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 306..414
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 427..527
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 532..639
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 642..744
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 749..849
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 856..954
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 960..1063
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1066..1169
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1174..1266
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1279..1379
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1384..1485
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1489..1586
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1589..1692
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1696..1797
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1801..1904
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1910..2010
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2017..2078
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT DOMAIN 2218..2328
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 2..278
FT /note="Actin-binding"
FT REGION 2080..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2333..2388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2080..2099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2124..2169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2367..2388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O15020"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15020"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 2169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15020"
FT MOD_RES 2359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15020"
FT CONFLICT 326..328
FT /note="VTL -> GTF (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="L -> F (in Ref. 2; BAA32473)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="D -> G (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="L -> P (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="V -> I (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="D -> G (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156..1157
FT /note="EL -> GA (in Ref. 2; BAA32473)"
FT /evidence="ECO:0000305"
FT CONFLICT 1194
FT /note="F -> V (in Ref. 2; BAA32473 and 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1555
FT /note="G -> R (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1769
FT /note="R -> W (in Ref. 3; AAG28596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2388 AA; 271064 MW; 3EC8966AF0665F19 CRC64;
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK
KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG ETLPKPTKGR MRIHCLENVD
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD
ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA
FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
MEAEHLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
VQAVDAVAAE LAAEHYHDIK RIAARQNNVA RLWDFLREMV AARRERLLLN LELQKVFQDL
LYLMDWMAEM KGRLQSQDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP
GKEYRPCDPQ LVSERVATLE QSYEALCELA ATRRARLEES RRLWRFLWEV GEAEAWVREQ
QHLLASAETG RDLTGVLRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGANQAST
RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPEVGHDEF
STQALARQHR ALEEEIRAHR PTLDALREQA AALPPALSHT PEVQGRVPTL EQHYEELQAR
AGERARALEA ALAFYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
MNALAARVTA VSDIAEQLLK ASPPGKDRII GTQEQLNQRW QQFRSLADGK KAALTSALSI
QNYHLECTET QAWMREKTKV IESTQDLGND LAGVLALQRK LAGTERDLEA ISARVGELTQ
EANALAAGHP AQAPAINTRL GEVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRTLGEE VTRDQADPQC
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYFLSHTEM
PGTLQAADAA IKKLEDFMST MDANGERIRG LLEAGRQLVS KGNIHAEKIQ EKADSIEKRH
RKNQEAVQQL LGRLRDNREQ QHFLQDCQEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ
AFMAELAANK DWLDKVDKEG RELTLEKPEL KVLVSEKLED LHRRWDELET TTQAKARSLF
DANRAELFAQ SCSALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLER EMAVREKEVE
AIQAQAKALA QEDQSAGEVE RTSRAVEEKF RALCQPMKDR CRRLQASREQ HQFHRDVEDE
ILWVTERLPM ASSLEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLKER QRTLGTAAAG
PELAELQEMW KRLSHELELR GKRLEEALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE
LSAQAEVKKH QVLEQALADY AQTIKQLAAS SQDMIDHEHP ESTRLTIRQA QVDKLYAGLK
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSTQVQQVQ
DDGLRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM
LWMDGINLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSACIDMG QELLARNHYA
AEEISEKLSQ LQSRRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE
LGCTVDEVES LIKRHEAFQK SAVAWEERFS ALEKLTALEE RENEQKRKRE EEERRKQPPT
SEPMASQPEG SLVDGQRVLD TAWDGTQSKL PPSTQAPSIN GVCTDTESSQ PLLEQQRLEQ
SNVPEGPGSG TGDESSGPRG ERQTLPRGPA PSPMPQSRSS ESAHVATLPA RGAELSAQEQ
MEGTLCRKQE MEAFNKKAAN RSWQNVYCVL RRGSLGFYKD ARAASAGVPY HGEVPVSLAR
AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP
VVPSASRGLT RAMTMPPVSQ PEGSIVLRSK DGREREREKR FSFFKKNK
