CAMP2_MOUSE
ID CAMP2_MOUSE Reviewed; 1461 AA.
AC Q8C1B1; B7ZNI4; Q80TK8; Q8C4J5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305};
DE AltName: Full=Calmodulin-regulated spectrin-associated protein 1-like protein 1;
GN Name=Camsap2 {ECO:0000312|MGI:MGI:1922434};
GN Synonyms=Camsap1l1, Kiaa1078 {ECO:0000303|PubMed:12693553};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1185 (ISOFORMS 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1223-1461 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
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 MRNA] OF 658-1461 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-393; THR-401;
RP SER-439; SER-573; SER-585; THR-652; SER-654; SER-836; SER-1120; SER-1285;
RP SER-1291 AND SER-1293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
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).
RN [7]
RP FUNCTION, AND INTERACTION WITH CAMSAP3.
RX PubMed=23169647; DOI=10.1073/pnas.1218017109;
RA Tanaka N., Meng W., Nagae S., Takeichi M.;
RT "Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of
RT noncentrosomal microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=32482850; DOI=10.1073/pnas.1907335117;
RA Robinson A.M., Takahashi S., Brotslaw E.J., Ahmad A., Ferrer E.,
RA Procissi D., Richter C.P., Cheatham M.A., Mitchell B.J., Zheng J.;
RT "CAMSAP3 facilitates basal body polarity and the formation of the central
RT pair of microtubules in motile cilia.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:13571-13579(2020).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization (PubMed:23169647). Specifically recognizes
CC growing microtubule minus-ends and autonomously decorates and
CC stabilizes microtubule lattice formed by microtubule minus-end
CC polymerization (By similarity). Acts on free microtubule minus-ends
CC that are not capped by microtubule-nucleating proteins or other factors
CC and protects microtubule minus-ends from depolymerization (By
CC similarity). In addition, it also reduces the velocity of microtubule
CC polymerization (By similarity). Through the microtubule cytoskeleton,
CC also regulates the organization of cellular organelles including the
CC Golgi and the early endosomes (By similarity). Essential for the
CC tethering, but not for nucleation of non-centrosomal microtubules at
CC the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP,
CC required to tether non-centrosomal minus-end microtubules to the Golgi,
CC an important step for polarized cell movement (By similarity). Also
CC acts as a regulator of neuronal polarity and development: localizes to
CC non-centrosomal microtubule minus-ends in neurons and stabilizes non-
CC centrosomal microtubules, which is required for neuronal polarity, axon
CC specification and dendritic branch formation (By similarity). Through
CC the microtubule cytoskeleton, regulates the autophagosome transport (By
CC similarity). {ECO:0000250|UniProtKB:Q08AD1}.
CC -!- SUBUNIT: Interacts with CAMSAP3 (PubMed:23169647). Interacts with
CC KATNA1 and KATNB1; leading to regulate the length of CAMSAP2-decorated
CC microtubule stretches (By similarity). Interacts with a complex formed
CC by AKAP9 and PDE4DIP isoform 2/MMG8/SMYLE, which recruits CAMSAP2 to
CC the Golgi (By similarity). Interacts with MAPRE1/EB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q08AD1, ECO:0000269|PubMed:23169647}.
CC -!- INTERACTION:
CC Q8C1B1; Q80VC9: Camsap3; NbExp=2; IntAct=EBI-8839434, EBI-2125556;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q08AD1}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q08AD1}. Cytoplasm
CC {ECO:0000269|PubMed:32482850}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:32482850}. Note=Associated with the minus-end
CC of microtubules and also detected at the centrosomes. Decorates the
CC minus-end of microtubules by decreasing the rate of tubulin
CC incorporation and remaining bound. The length of CAMSAP2-decorated
CC stretches on the minus-end of microtubules is dependent on MAPRE1/EB1
CC and MAPRE3/EB3, which promote elongation of CAMSAP2-decorated
CC microtubule stretches. Recruited to the Golgi apparatus by AKAP9 and
CC PDE4DIP isoform 2/MMG8/SMYLE. In neurons, localizes to the minus-end of
CC microtubules in axon and dendrites. {ECO:0000250|UniProtKB:Q08AD1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C1B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C1B1-2; Sequence=VSP_030807;
CC -!- DOMAIN: The CKK domain binds microtubules and specifically recognizes
CC the minus-end of microtubules. {ECO:0000250|UniProtKB:Q08AD1,
CC ECO:0000255|PROSITE-ProRule:PRU00841}.
CC -!- DOMAIN: The MBD (microtubule-binding domain) region can recognize some
CC features of the microtubule lattice, which might contribute to the
CC specific decoration of growing microtubule minus-ends by CAMSAP2.
CC {ECO:0000250|UniProtKB:Q08AD1}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; BC145258; AAI45259.1; -; mRNA.
DR EMBL; AK028542; BAC25999.2; -; mRNA.
DR EMBL; AK081975; BAC38384.1; -; mRNA.
DR EMBL; AK122436; BAC65718.1; -; mRNA.
DR CCDS; CCDS83597.1; -. [Q8C1B1-1]
DR RefSeq; NP_001334039.1; NM_001347110.1. [Q8C1B1-1]
DR RefSeq; XP_006529897.1; XM_006529834.2. [Q8C1B1-2]
DR AlphaFoldDB; Q8C1B1; -.
DR SMR; Q8C1B1; -.
DR BioGRID; 212510; 7.
DR DIP; DIP-60092N; -.
DR IntAct; Q8C1B1; 3.
DR STRING; 10090.ENSMUSP00000041920; -.
DR iPTMnet; Q8C1B1; -.
DR PhosphoSitePlus; Q8C1B1; -.
DR SwissPalm; Q8C1B1; -.
DR EPD; Q8C1B1; -.
DR jPOST; Q8C1B1; -.
DR MaxQB; Q8C1B1; -.
DR PaxDb; Q8C1B1; -.
DR PeptideAtlas; Q8C1B1; -.
DR PRIDE; Q8C1B1; -.
DR ProteomicsDB; 265519; -. [Q8C1B1-1]
DR ProteomicsDB; 265520; -. [Q8C1B1-2]
DR Antibodypedia; 20635; 79 antibodies from 19 providers.
DR Ensembl; ENSMUST00000192001; ENSMUSP00000142166; ENSMUSG00000041570. [Q8C1B1-1]
DR GeneID; 67886; -.
DR KEGG; mmu:67886; -.
DR UCSC; uc007cur.2; mouse. [Q8C1B1-1]
DR UCSC; uc011wsz.1; mouse. [Q8C1B1-2]
DR CTD; 23271; -.
DR MGI; MGI:1922434; Camsap2.
DR VEuPathDB; HostDB:ENSMUSG00000041570; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; Q8C1B1; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; Q8C1B1; -.
DR BioGRID-ORCS; 67886; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Camsap2; mouse.
DR PRO; PR:Q8C1B1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C1B1; protein.
DR Bgee; ENSMUSG00000041570; Expressed in otolith organ and 227 other tissues.
DR ExpressionAtlas; Q8C1B1; baseline and differential.
DR Genevisible; Q8C1B1; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:1990752; C:microtubule end; ISO:MGI.
DR GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:MGI.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0033043; P:regulation of organelle organization; IGI:UniProtKB.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1461
FT /note="Calmodulin-regulated spectrin-associated protein 2"
FT /id="PRO_0000316833"
FT DOMAIN 211..324
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1321..1455
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 361..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1007
FT /note="MBD region"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT REGION 921..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 730..767
FT /evidence="ECO:0000255"
FT COILED 861..900
FT /evidence="ECO:0000255"
FT COILED 1138..1210
FT /evidence="ECO:0000255"
FT COMPBIAS 573..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 970
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 975
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 977
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1257
FT /note="P -> PGSRISRVFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_030807"
FT CONFLICT 30
FT /note="A -> T (in Ref. 1; AAI45259)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="R -> Q (in Ref. 1; AAI45259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1461 AA; 164333 MW; 24308DADC498788A CRC64;
MGDAADPREM RRTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELGDPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MISIEKVIAC AQQYSAFFQA TDLPYDIEDA
VMYWMNKVNE HLKDIMEQEQ KSKEHHPAEA PGGQKARYRK EQTLLKQLPC IPLVENLLKD
GTDGCALAAL IHFYCPAVVR LEDICLKETM SLADSLYNLQ LIQEFCQEYL NHCCHFSLED
MLYAASSIKS NYLVFMAELF WWFEVVKPSF VQPRVVRPQG AEPAKDVPSV PVLNAAKRNI
RDSSSSSDFS SRYTRPQTHS SASGGIRRSS SMSYVDGFIG TWPKEKRTSV HGVSFDISFD
KEDSAQSSTP NRGIIRSVSN EGLTLNNSRA SKHIRKNLSF KPVNGEEEES IEEELHVDPH
GDLQSPMPLN TNELNSNEST HYKLPNGALQ NRVLLDEFGN QIETPSIEEA LQIIHDTERP
PHTPRPDQIA NGFFLHGQDL SILNSNIKLN QSSPDNLTDT KGALSPITDT TEVDTGIHVP
SEDIPETMDE DSSLRDYTVS LDSDMDDASK LLQDYDLRAS NPREALSPCP STISTKSQPG
SSASSSSGVK MTSFAEQKFR KLNHTDGKSS GSSSQKTTPE GSELNIPHVV SWAQIPEEAG
VAPGRDTTQL LASEMVHLRM RLEEKRRAIE AQKKKMEAAF TKQRQKMGRT AFLTVVKKKG
EGISPLREEA AGAEDEKVYT DRAKERESQK MDGQRSKSLA DIKESMETPP GRWLKSPTTP
VDPERQWNLT SPSEETLNEG EILEYTKSIE KLNSSLHFLQ QEMQRLSLQQ EMLMQMREQQ
AWVISPPQPS PQKQIRDFKP RQAGLSSAAA PFSSDSPRPT HPSPQSSTRK SASFSVKNQR
TPRPNELKIT PLNRTLTPPR SVDSLPRLRR FSPSQVPIQT RSFVCFGDDG EPQKEPKQKE
EIKKEPSECK GTLGPCDHNP GEKEIKPVES TVSEVLSQPI TETVCVTPNE DQLSQPTEPP
PKPVFPPTAP KNVNLIEVSL SDLKPPEKAD VSVEKLDGES DKEQFDDDQK VCCGFFFKDD
QKAENDMAMK RAALLEKRLR REKETQLRKQ QLEAEMEHKK EETRRKTEEE RQKKEDERAR
REFIRQEYMR RKQLKLMEDM DTVIKPRPQA AKQKKQRPKS IHRDHIESPK TPIKGPPVSS
LSLASLNTGD SESVHSGKRT PRSESVEGFL SPSRCGSRNG EKDWENASTT SSVASGTEYT
GPKLYKEPSA KSNKHIIQNA LAHCCLAGKV NEGQKKKILE EMEKSDANNF LILFRDSGCQ
FRSLYTYCPE TEEINKLTGI GPKSITKKMI EGLYKYNSDR KQFSHIPAKT LSASVDAITI
HSHLWQTKRP VTPKKLLPTK A
