ID BICD2_MOUSE Reviewed; 820 AA. AC Q921C5; Q80TU1; Q8BTE3; Q9DCL3; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 158. DE RecName: Full=Protein bicaudal D homolog 2; DE Short=Bic-D 2; GN Name=Bicd2; Synonyms=Kiaa0699; 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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DCTN2, RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=11483508; DOI=10.1093/emboj/20.15.4041; RA Hoogenraad C.C., Akhmanova A., Howell S.A., Dortland B.R., de Zeeuw C.I., RA Willemsen R., Visser P., Grosveld F., Galjart N.; RT "Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin RT pathway by interacting with these complexes."; RL EMBO J. 20:4041-4054(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; 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 [4] RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney; 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 [5] RP FUNCTION, INTERACTION WITH RAB6A, AND SUBCELLULAR LOCATION. RX PubMed=12447383; DOI=10.1038/ncb891; RA Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T., RA Galjart N., Grosveld F., Goud B., De Zeeuw C.I., Barnekow A., RA Hoogenraad C.C.; RT "Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the RT dynein-dynactin motor complex."; RL Nat. Cell Biol. 4:986-992(2002). RN [6] RP INTERACTION WITH CPNE4. RX PubMed=12522145; DOI=10.1074/jbc.m212632200; RA Tomsig J.L., Snyder S.L., Creutz C.E.; RT "Identification of targets for calcium signaling through the copine family RT of proteins. Characterization of a coiled-coil copine-binding motif."; RL J. Biol. Chem. 278:10048-10054(2003). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, 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 [9] RP FUNCTION, AND INTERACTION WITH RANBP2; RAB6A AND KIF5A. RX PubMed=20386726; DOI=10.1371/journal.pbio.1000350; RA Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A., Yu K.L., RA Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N., Demmers J., RA Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H., Akhmanova A.; RT "Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes RT and regulate centrosome and nuclear positioning during mitotic entry."; RL PLoS Biol. 8:E1000350-E1000350(2010). RN [10] RP FUNCTION, AND INTERACTION WITH DYNLL1; DYNC1H1; DYNC1I2; DCTN1 AND DCTN2. RX PubMed=22956769; DOI=10.1091/mbc.e12-03-0210; RA Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I., RA Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C., RA King S.J., Akhmanova A.; RT "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to RT cellular structures."; RL Mol. Biol. Cell 23:4226-4241(2012). RN [11] RP TISSUE SPECIFICITY. RX PubMed=23664119; DOI=10.1016/j.ajhg.2013.04.013; RA Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., RA Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., RA Ooms T., Timmerman V., Tournev I., Jordanova A.; RT "Molecular defects in the motor adaptor BICD2 cause proximal spinal RT muscular atrophy with autosomal-dominant inheritance."; RL Am. J. Hum. Genet. 92:955-964(2013). RN [12] RP FUNCTION, AND COMPLEX FORMATION WITH DYNEIN AND DYNACTIN. RX PubMed=24986880; DOI=10.15252/embj.201488792; RA Schlager M.A., Hoang H.T., Urnavicius L., Bullock S.L., Carter A.P.; RT "In vitro reconstitution of a highly processive recombinant human dynein RT complex."; RL EMBO J. 33:1855-1868(2014). RN [13] RP FUNCTION. RX PubMed=25035494; DOI=10.1126/science.1254198; RA McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.; RT "Activation of cytoplasmic dynein motility by dynactin-cargo adapter RT complexes."; RL Science 345:337-341(2014). RN [14] RP FUNCTION, INTERACTION WITH RAB6A, AND SUBCELLULAR LOCATION. RX PubMed=25962623; DOI=10.1016/j.bbamcr.2015.05.005; RA Matsuto M., Kano F., Murata M.; RT "Reconstitution of the targeting of Rab6A to the Golgi apparatus in semi- RT intact HeLa cells: A role of BICD2 in stabilizing Rab6A on Golgi membranes RT and a concerted role of Rab6A/BICD2 interactions in Golgi-to-ER retrograde RT transport."; RL Biochim. Biophys. Acta 1853:2592-2609(2015). RN [15] RP ASSOCIATION WITH MICROTUBULES. RX PubMed=26968983; DOI=10.15252/embj.201593071; RA McKenney R.J., Huynh W., Vale R.D., Sirajuddin M.; RT "Tyrosination of alpha-tubulin controls the initiation of processive RT dynein-dynactin motility."; RL EMBO J. 35:1175-1185(2016). CC -!- FUNCTION: Acts as an adapter protein linking the dynein motor complex CC to various cargos and converts dynein from a non-processive to a highly CC processive motor in the presence of dynactin. Facilitates and CC stabilizes the interaction between dynein and dynactin and activates CC dynein processivity (the ability to move along a microtubule for a long CC distance without falling off the track) (PubMed:11483508, CC PubMed:25035494, PubMed:24986880, PubMed:22956769). Facilitates the CC binding of RAB6A to the Golgi by stabilizing its GTP-bound form CC (PubMed:25962623). Regulates coat complex coatomer protein I (COPI)- CC independent Golgi-endoplasmic reticulum transport via its interaction CC with RAB6A and recruitment of the dynein-dynactin motor complex CC (PubMed:12447383, PubMed:25962623). Contributes to nuclear and CC centrosomal positioning prior to mitotic entry through regulation of CC both dynein and kinesin-1. During G2 phase of the cell cycle, CC associates with RANBP2 at the nuclear pores and recruits dynein and CC dynactin to the nuclear envelope to ensure proper positioning of the CC nucleus relative to centrosomes prior to the onset of mitosis CC (PubMed:20386726). {ECO:0000269|PubMed:11483508, CC ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:20386726, CC ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880, CC ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623}. CC -!- SUBUNIT: Part of a tripartite complex with dynein and dynactin, acts an CC adapter linking the dynein motor complex and dynactin (By similarity). CC Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts CC with NEK9 (By similarity). Interacts with DCTN2 (PubMed:11483508, CC PubMed:22956769). Interacts with RAB6A (PubMed:12447383, CC PubMed:25962623). Interacts with DNAI1 (By similarity). Interacts with CC DYNLL1, DYNC1H1, DYNC1I2 and DCTN1 (PubMed:22956769). Forms a complex CC with dynein and dynactin (PubMed:24986880). The dynein-dynactin-BICD2 CC ternary complex (DDB) binds preferentially to tyrosinated microtubules CC than to detyrosinated microtubules (PubMed:26968983). Interacts with CC RANBP2, RAB6A and KIF5A (PubMed:20386726). Interacts with KIF1C (By CC similarity). {ECO:0000250|UniProtKB:Q8TD16, CC ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, CC ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:20386726, CC ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880, CC ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623, CC ECO:0000269|PubMed:26968983}. CC -!- INTERACTION: CC Q921C5; P35279: Rab6a; NbExp=3; IntAct=EBI-642984, EBI-444674; CC Q921C5-1; P49792: RANBP2; Xeno; NbExp=4; IntAct=EBI-642995, EBI-973138; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11483508, CC ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:25962623}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:11483508}. Cytoplasm CC {ECO:0000250|UniProtKB:Q8TD16}. Nucleus, nuclear pore complex CC {ECO:0000250|UniProtKB:Q8TD16}. Nucleus envelope CC {ECO:0000250|UniProtKB:Q8TD16}. Note=In interphase cells mainly CC localizes to the Golgi complex and colocalizes with dynactin at CC microtubule plus ends (PubMed:11483508). Localizes to the nuclear CC envelope and cytoplasmic stacks of nuclear pore complex known as CC annulate lamellae in a RANBP2-dependent manner during G2 phase of the CC cell cycle (By similarity). {ECO:0000250|UniProtKB:Q8TD16, CC ECO:0000269|PubMed:11483508}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q921C5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q921C5-2; Sequence=VSP_007970; CC Name=3; CC IsoId=Q921C5-3; Sequence=VSP_007971, VSP_007972; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the CC spinal cord. {ECO:0000269|PubMed:23664119}. CC -!- DOMAIN: The fourth coiled coil region is involved in Golgi targeting CC and in the interaction with DCTN2. {ECO:0000269|PubMed:11483508}. CC -!- PTM: Phosphorylated by NEK9 in vitro. {ECO:0000250|UniProtKB:Q8TD16}. CC -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65630.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB22282.1; Type=Frameshift; Evidence={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; AJ250106; CAC51393.1; -; mRNA. DR EMBL; AK122348; BAC65630.1; ALT_INIT; mRNA. DR EMBL; BC032198; AAH32198.1; -; mRNA. DR EMBL; AK002683; BAB22282.1; ALT_FRAME; mRNA. DR EMBL; AK003456; BAC25035.1; -; mRNA. DR CCDS; CCDS36656.1; -. [Q921C5-1] DR CCDS; CCDS36657.1; -. [Q921C5-2] DR RefSeq; NP_001034268.1; NM_001039179.2. [Q921C5-2] DR RefSeq; NP_001034269.1; NM_001039180.2. DR RefSeq; NP_084067.1; NM_029791.4. [Q921C5-1] DR AlphaFoldDB; Q921C5; -. DR SMR; Q921C5; -. DR BioGRID; 218383; 22. DR DIP; DIP-49453N; -. DR IntAct; Q921C5; 20. DR MINT; Q921C5; -. DR STRING; 10090.ENSMUSP00000039394; -. DR iPTMnet; Q921C5; -. DR PhosphoSitePlus; Q921C5; -. DR SwissPalm; Q921C5; -. DR EPD; Q921C5; -. DR jPOST; Q921C5; -. DR MaxQB; Q921C5; -. DR PaxDb; 10090-ENSMUSP00000039394; -. DR PeptideAtlas; Q921C5; -. DR ProteomicsDB; 273741; -. [Q921C5-1] DR ProteomicsDB; 273742; -. [Q921C5-2] DR ProteomicsDB; 273743; -. [Q921C5-3] DR Pumba; Q921C5; -. DR Antibodypedia; 13783; 226 antibodies from 27 providers. DR Ensembl; ENSMUST00000048544.14; ENSMUSP00000039394.7; ENSMUSG00000037933.17. [Q921C5-2] DR Ensembl; ENSMUST00000110085.11; ENSMUSP00000105712.4; ENSMUSG00000037933.17. [Q921C5-1] DR GeneID; 76895; -. DR KEGG; mmu:76895; -. DR UCSC; uc007qjg.2; mouse. [Q921C5-1] DR UCSC; uc007qji.2; mouse. [Q921C5-2] DR AGR; MGI:1924145; -. DR CTD; 23299; -. DR MGI; MGI:1924145; Bicd2. DR VEuPathDB; HostDB:ENSMUSG00000037933; -. DR eggNOG; KOG0999; Eukaryota. DR GeneTree; ENSGT00940000154471; -. DR InParanoid; Q921C5; -. DR OMA; CACASER; -. DR OrthoDB; 5350043at2759; -. DR PhylomeDB; Q921C5; -. DR TreeFam; TF323833; -. DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR BioGRID-ORCS; 76895; 5 hits in 77 CRISPR screens. DR ChiTaRS; Bicd2; mouse. DR PRO; PR:Q921C5; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q921C5; Protein. DR Bgee; ENSMUSG00000037933; Expressed in rostral migratory stream and 266 other cell types or tissues. DR ExpressionAtlas; Q921C5; baseline and differential. DR GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro. DR GO; GO:0034452; F:dynactin binding; IDA:UniProtKB. DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB. DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:FlyBase. DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL. DR GO; GO:0051642; P:centrosome localization; ISS:UniProtKB. DR GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; IMP:BHF-UCL. DR GO; GO:0007018; P:microtubule-based movement; IDA:MGI. DR GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; IMP:BHF-UCL. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB. DR Gene3D; 6.10.250.2470; -; 1. DR InterPro; IPR018477; BICD. DR PANTHER; PTHR31233; BICAUDAL D FAMILY MEMBER; 1. DR PANTHER; PTHR31233:SF7; PROTEIN BICAUDAL D HOMOLOG 2; 1. DR Pfam; PF09730; BicD; 1. DR Genevisible; Q921C5; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW Golgi apparatus; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Translocation; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT CHAIN 2..820 FT /note="Protein bicaudal D homolog 2" FT /id="PRO_0000205360" FT REGION 25..400 FT /note="Interaction with DYNLL1, DYNC1H1, DYNC1I2, DCTN1 and FT DCTN2" FT /evidence="ECO:0000269|PubMed:22956769" FT REGION 313..332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 336..595 FT /note="Interaction with KIF5A" FT /evidence="ECO:0000269|PubMed:20386726" FT REGION 400..427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 563..582 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 586..820 FT /note="Interaction with RANBP2" FT /evidence="ECO:0000269|PubMed:20386726" FT REGION 591..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 662..810 FT /note="Interaction with RAB6A" FT /evidence="ECO:0000269|PubMed:12447383, FT ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:25962623" FT REGION 799..820 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 20..270 FT /evidence="ECO:0000255" FT COILED 340..539 FT /evidence="ECO:0000255" FT COILED 662..804 FT /evidence="ECO:0000255" FT COMPBIAS 406..427 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..613 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 321 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 345 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 570 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 578 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 598 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT MOD_RES 819 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TD16" FT VAR_SEQ 328..338 FT /note="APPSPSLVSDL -> VHPLHALCLTV (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_007971" FT VAR_SEQ 339..820 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_007972" FT VAR_SEQ 820 FT /note="L -> VSHTCACASERAEGAGLANQVFCSEKHSIYCD (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:12693553" FT /id="VSP_007970" SQ SEQUENCE 820 AA; 93391 MW; 0C1A1754CD74DDE1 CRC64; MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV LEEKHQLKLQ FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE ESLIQESASK EQYYVRKVLE LQTELKQLRN VLTNTQSENE RLTSVAQELK EINQNVEIQR GRLRDDIKEY KFREARLLQD YSELEEENIS LQKQVSVLRQ NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL EEALETLKTE REQKNNLRKE LSHYMSINDS FYTSHLQVSL DGLKFSDDTV TAEPNNDAEA LVNGFEHSGL VKSSLDNKTS TPRKDGLAPP SPSLVSDLLS ELHISEIQKL KQQLVQMERE KVGLLATLQD TQKQLEQARG TLSEQHEKVN RLTENLSALR RLQAGKERQT SLDNEKDRDS HEDGDYYEVD INGPEILACK YHVAVAEAGE LREQLKALRS THEAREAQHA EEKGRYEAEG QALTEKISLL EKASHQDREL LAHLEKELKK VSDVAGETQG SLNVAQDELV TFSEELANLY HHVCMCNNET PNRVMLDYYR EGQGKAGRTS PEGRGRRSPV LLPKGLLATE VGRADGGTGD NSPSPSSSLP SPLSDPRREP MNIYNLIAII RDQIKHLQAA VDRTTELSRQ RIASQELGPA VDKDKEALME EILKLKSLLS TKREQITTLR TVLKANKQTA EVALANLKSK YENEKAMVTE TMMKLRNELK ALKEDAATFS SLRAMFATRC DEYITQLDEM QRQLAAAEDE KKTLNSLLRM AIQQKLALTQ RLELLELDHE QTRRGRSKAA SKAKPASPSL //