BICD2_MOUSE
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 03-AUG-2022, entry version 150.
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: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
CC Interacts with NEK9 (By similarity). Interacts with DCTN2
CC (PubMed:11483508, PubMed:22956769). Interacts with RAB6A
CC (PubMed:12447383, PubMed:25962623). Interacts with DNAI1 (By
CC similarity). Interacts with DYNLL1, DYNC1H1, DYNC1I2 and DCTN1
CC (PubMed:22956769). Forms a complex with dynein and dynactin
CC (PubMed:24986880). The dynein-dynactin-BICD2 ternary complex (DDB)
CC binds preferentially to tyrosinated microtubules than to detyrosinated
CC microtubules (PubMed:26968983). Interacts with RANBP2, RAB6A and KIF5A
CC (PubMed:20386726). Interacts with KIF1C (By similarity).
CC {ECO:0000250|UniProtKB:Q8TD16, ECO:0000269|PubMed:11483508,
CC ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:12522145,
CC ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22956769,
CC ECO:0000269|PubMed:24986880, ECO:0000269|PubMed:25035494,
CC ECO:0000269|PubMed:25962623, 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 CAUTION: [Isoform 3]:
CC Sequence=BAB22282.1; Type=Frameshift; Evidence={ECO:0000305};
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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; 19.
DR DIP; DIP-49453N; -.
DR IntAct; Q921C5; 19.
DR MINT; Q921C5; -.
DR STRING; 10090.ENSMUSP00000039394; -.
DR iPTMnet; Q921C5; -.
DR PhosphoSitePlus; Q921C5; -.
DR EPD; Q921C5; -.
DR jPOST; Q921C5; -.
DR MaxQB; Q921C5; -.
DR PaxDb; Q921C5; -.
DR PeptideAtlas; Q921C5; -.
DR PRIDE; Q921C5; -.
DR ProteomicsDB; 273741; -. [Q921C5-1]
DR ProteomicsDB; 273742; -. [Q921C5-2]
DR ProteomicsDB; 273743; -. [Q921C5-3]
DR Antibodypedia; 13783; 208 antibodies from 27 providers.
DR Ensembl; ENSMUST00000048544; ENSMUSP00000039394; ENSMUSG00000037933. [Q921C5-2]
DR Ensembl; ENSMUST00000110085; ENSMUSP00000105712; ENSMUSG00000037933. [Q921C5-1]
DR GeneID; 76895; -.
DR KEGG; mmu:76895; -.
DR UCSC; uc007qjg.2; mouse. [Q921C5-1]
DR UCSC; uc007qji.2; mouse. [Q921C5-2]
DR CTD; 23299; -.
DR MGI; MGI:1924145; Bicd2.
DR VEuPathDB; HostDB:ENSMUSG00000037933; -.
DR eggNOG; KOG0999; Eukaryota.
DR GeneTree; ENSGT00940000154471; -.
DR InParanoid; Q921C5; -.
DR OMA; AYTNHRK; -.
DR OrthoDB; 542877at2759; -.
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 72 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 264 other tissues.
DR ExpressionAtlas; Q921C5; baseline and differential.
DR Genevisible; Q921C5; MM.
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:0033365; P:protein localization to organelle; IBA:GO_Central.
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 InterPro; IPR018477; BICD.
DR PANTHER; PTHR31233; PTHR31233; 1.
DR Pfam; PF09730; BicD; 1.
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
