ID SPTA2_MOUSE Reviewed; 2472 AA. AC P16546; A3KGU6; Q8K380; Q9CT05; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 4. DT 16-JUN-2009, entry version 99. DE RecName: Full=Spectrin alpha chain, brain; DE AltName: Full=Spectrin, non-erythroid alpha chain; DE AltName: Full=Alpha-II spectrin; DE AltName: Full=Fodrin alpha chain; GN Name=Sptan1; Synonyms=Spna2, Spta2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RG The mouse genome sequencing consortium; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 8-18; 46-51; 64-81; 85-121; 130-137; 169-227; RP 251-259; 263-272; 275-295; 321-347; 382-402; 419-439; 442-459; RP 523-547; 614-627; 686-708; 734-742; 792-801; 813-839; 847-862; RP 908-930; 990-1002; 1013-1022; 1068-1082; 1197-1209; 1253-1273; RP 1314-1326; 1350-1359; 1370-1380; 1418-1427; 1501-1519; 1547-1570; RP 1592-1605; 1608-1619; 1700-1713; 1716-1736; 1772-1781; 1784-1794; RP 1808-1828; 1830-1844; 1866-1923; 1926-1938; 1985-1995; 2018-2040; RP 2065-2075; 2088-2098; 2138-2155; 2265-2281; 2354-2382; 2405-2435 AND RP 2455-2467, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 995-1396 (ISOFORM 2). RC TISSUE=Macrophage; RX MEDLINE=90254195; PubMed=2111175; DOI=10.1016/0300-9084(90)90168-G; RA Sri Widada J., Asselin J., Colote S., Ferraz C., Trave G., Afshar M., RA Haiech J., Liautard J.-P.; RT "Identification of the calmodulin binding domain of alpha-fodrin and RT implications for folding."; RL Biochimie 72:19-24(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 995-1396 (ISOFORM 2). RX MEDLINE=89178662; PubMed=2926814; DOI=10.1016/0022-2836(89)90355-0; RA Sri Widada J., Asselin J., Colote S., Marti J., Ferraz C., Trave G., RA Haiech J., Liautard J.-P.; RT "Cloning and deletion mutagenesis using direct protein-protein RT interaction on an expression vector. Identification of the calmodulin RT binding domain of alpha-fodrin."; RL J. Mol. Biol. 205:455-458(1989). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1118-2472. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1819-2472. RC STRAIN=C57BL/6J; TISSUE=Embryo; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [7] RP PROTEIN SEQUENCE OF 2071-2079. RC STRAIN=C57BL/6Cr; TISSUE=Brain; RX PubMed=10870971; RX DOI=10.1002/(SICI)1522-2683(20000501)21:9<1853::AID-ELPS1853>3.3.CO;2-P; RA Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T., RA Watanabe Y., Morimasa T., Hosokawa K., Toda T.; RT "Proteome analysis of mouse brain: two-dimensional electrophoresis RT profiles of tissue proteins during the course of aging."; RL Electrophoresis 21:1853-1871(2000). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND MASS RP SPECTROMETRY. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND MASS RP SPECTROMETRY. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Fodrin, which seems to be involved in secretion, CC interacts with calmodulin in a calcium-dependent manner and is CC thus candidate for the calcium-dependent movement of the CC cytoskeleton at the membrane. CC -!- SUBUNIT: Interacts with CALM (By similarity). Like erythrocyte CC spectrin, the spectrin-like proteins are capable of forming dimers CC which can further associate to tetramers. Interacts with ACP1. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell CC cortex. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P16546-1; Sequence=Displayed; CC Name=2; CC IsoId=P16546-2; Sequence=VSP_022093; CC -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage CC by calpain in vitro (By similarity). CC -!- SIMILARITY: Belongs to the spectrin family. CC -!- SIMILARITY: Contains 3 EF-hand domains. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 23 spectrin repeats. 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; AL928926; CAM46236.1; -; Genomic_DNA. DR EMBL; X12801; CAA31289.1; -; mRNA. DR EMBL; BC027791; AAH27791.1; ALT_INIT; mRNA. DR EMBL; AK011566; BAB27703.1; -; mRNA. DR IPI; IPI00753793; -. DR IPI; IPI00753815; -. DR PIR; A43769; A43769. DR PIR; PC7076; PC7076. DR UniGene; Mm.204969; -. DR UniGene; Mm.448063; -. DR HSSP; P07751; 1PWT. DR SMR; P16546; 1657-1974, 1873-1976. DR PhosphoSite; P16546; -. DR Ensembl; ENSMUSG00000057738; Mus musculus. DR MGI; MGI:98386; Spna2. DR HOVERGEN; P16546; -. DR ArrayExpress; P16546; -. DR Bgee; P16546; -. DR CleanEx; MM_SPNA2; -. DR GermOnline; ENSMUSG00000057738; Mus musculus. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI. DR GO; GO:0005916; C:fascia adherens; IDA:MGI. DR GO; GO:0030018; C:Z disc; IDA:MGI. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-KW. DR InterPro; IPR014837; EF-hand_Ca_insen. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR018248; EF_hand. DR InterPro; IPR018247; EF_HAND_1. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR013315; Spectrin_alpha_SH3. DR InterPro; IPR002017; Spectrin_repeat. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR Pfam; PF00036; efhand; 2. DR Pfam; PF08726; efhand_Ca_insen; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF00435; Spectrin; 20. DR PRINTS; PR01887; SPECTRNALPHA. DR ProDom; PD000012; EF-hand; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00054; EFh; 2. DR SMART; SM00326; SH3; 1. DR SMART; SM00150; SPEC; 20. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Actin capping; Actin-binding; Alternative splicing; Calcium; KW Calmodulin-binding; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Phosphoprotein; Repeat; SH3 domain. FT CHAIN 1 2472 Spectrin alpha chain, brain. FT /FTId=PRO_0000073456. FT REPEAT 10 42 Spectrin 1. FT REPEAT 44 147 Spectrin 2. FT REPEAT 149 253 Spectrin 3. FT REPEAT 255 359 Spectrin 4. FT REPEAT 361 465 Spectrin 5. FT REPEAT 467 571 Spectrin 6. FT REPEAT 573 676 Spectrin 7. FT REPEAT 678 782 Spectrin 8. FT REPEAT 784 888 Spectrin 9. FT REPEAT 890 955 Spectrin 10. FT DOMAIN 967 1026 SH3. FT REPEAT 1062 1089 Spectrin 11. FT REPEAT 1091 1161 Spectrin 12. FT REPEAT 1208 1231 Spectrin 13. FT REPEAT 1233 1337 Spectrin 14. FT REPEAT 1339 1443 Spectrin 15. FT REPEAT 1445 1549 Spectrin 16. FT REPEAT 1551 1656 Spectrin 17. FT REPEAT 1658 1762 Spectrin 18. FT REPEAT 1764 1868 Spectrin 19. FT REPEAT 1870 1974 Spectrin 20. FT REPEAT 1976 2081 Spectrin 21. FT REPEAT 2091 2195 Spectrin 22. FT REPEAT 2205 2310 Spectrin 23. FT DOMAIN 2323 2358 EF-hand 1. FT DOMAIN 2366 2401 EF-hand 2. FT DOMAIN 2404 2439 EF-hand 3. FT CA_BIND 2336 2347 1 (Potential). FT CA_BIND 2379 2390 2 (Potential). FT SITE 1176 1177 Cleavage; by mu-calpain (By similarity). FT MOD_RES 1029 1029 Phosphoserine. FT MOD_RES 1031 1031 Phosphoserine (By similarity). FT MOD_RES 1176 1176 Phosphotyrosine (By similarity). FT MOD_RES 1217 1217 Phosphoserine. FT MOD_RES 1323 1323 Phosphoserine (By similarity). FT MOD_RES 2423 2423 Phosphotyrosine (By similarity). FT VAR_SEQ 1053 1072 Missing (in isoform 2). FT /FTId=VSP_022093. FT CONFLICT 995 995 T -> A (in Ref. 3; CAA31289). FT CONFLICT 1156 1156 D -> G (in Ref. 3; CAA31289). FT CONFLICT 1204 1204 T -> S (in Ref. 3; CAA31289). FT CONFLICT 1279 1279 E -> D (in Ref. 3; CAA31289). FT CONFLICT 1396 1396 Q -> P (in Ref. 3; CAA31289). FT CONFLICT 1819 1819 A -> S (in Ref. 6; BAB27703). SQ SEQUENCE 2472 AA; 284597 MW; 7D778AC0B32D0AD6 CRC64; MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA AERHARLDDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA DESGQALLAA SHYASDEVRE KLSILSEERT ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQGQID NQTRITKEAG SVSLRMKQVE ELYQSLLELG EKRKGMLEKS CKKFMLFREA NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDHCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD TINGRFQKIK SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE HWKELKQLAA ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHIQ SKAIEARHAS LMKRWTQLLA NSATRKKKLL EAQSHFRKVE DLFLTFAKKA SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF DYVEFTRSLF VN //