SGIP1_MOUSE
ID SGIP1_MOUSE Reviewed; 806 AA.
AC Q8VD37; A7BFW0; Q3UFU3; Q3UGA0; Q8BXX4; Q8C034; Q9CXT2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1;
DE AltName: Full=Endophilin-3-interacting protein;
GN Name=Sgip1;
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 6), FUNCTION IN ENDOCYTOSIS,
RP LIPID-BINDING, SUBCELLULAR LOCATION, AND INTERACTION WITH AP2A1 AND EPS15.
RX PubMed=17626015; DOI=10.1074/jbc.m703815200;
RA Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K.,
RA Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.;
RT "SGIP1alpha is an endocytic protein that directly interacts with
RT phospholipids and Eps15.";
RL J. Biol. Chem. 282:26481-26489(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryonic head, Melanoma, and Olfactory bulb;
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] (ISOFORM 1).
RC TISSUE=Retina;
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 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 INDUCTION.
RX PubMed=15919751; DOI=10.1210/en.2005-0282;
RA Trevaskis J., Walder K., Foletta V., Kerr-Bayles L., McMillan J.,
RA Cooper A., Lee S., Bolton K., Prior M., Fahey R., Whitecross K.,
RA Morton G.J., Schwartz M.W., Collier G.R.;
RT "Src homology 3-domain growth factor receptor-bound 2-like (endophilin)
RT interacting protein 1, a novel neuronal protein that regulates energy
RT balance.";
RL Endocrinology 146:3757-3764(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-149; SER-151;
RP SER-156; THR-180; THR-182; THR-247; THR-259; SER-265; SER-287; SER-289;
RP SER-300; SER-316; SER-319; THR-324; THR-328; SER-371; SER-398; THR-409 AND
RP SER-484, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274 (ISOFORMS 3 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 (ISOFORM 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 (ISOFORM 7), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Lung;
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 [8]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 7), INTERACTION WITH CANX, AND
RP TISSUE SPECIFICITY.
RX PubMed=21747946; DOI=10.1371/journal.pone.0021678;
RA Li H.D., Liu W.X., Michalak M.;
RT "Enhanced clathrin-dependent endocytosis in the absence of calnexin.";
RL PLoS ONE 6:E21678-E21678(2011).
CC -!- FUNCTION: May function in clathrin-mediated endocytosis. Has both a
CC membrane binding/tubulating activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides and is required for the endocytosis of the
CC transferrin receptor. May also bind tubulin. May play a role in the
CC regulation of energy homeostasis. {ECO:0000269|PubMed:17626015,
CC ECO:0000269|PubMed:21747946}.
CC -!- SUBUNIT: Interacts with proteins essential or regulating the formation
CC of functional clathrin-coated pits (Probable). Interacts with CANX
CC (PubMed:17626015, PubMed:21747946). Interacts with AP2A1
CC (PubMed:17626015). Interacts with EPS15 (PubMed:17626015). Interacts
CC with SH3GL3 (By similarity). Interacts with AMPH (By similarity).
CC Interacts with ITSN1 (via SH3 domains) (By similarity). Interacts with
CC and REPS1 (By similarity). {ECO:0000250|UniProtKB:Q9BQI5,
CC ECO:0000269|PubMed:17626015, ECO:0000269|PubMed:21747946, ECO:0000305}.
CC -!- INTERACTION:
CC Q8VD37; P35564: Canx; NbExp=3; IntAct=EBI-776269, EBI-738422;
CC Q8VD37; A7BFV9; Xeno; NbExp=4; IntAct=EBI-776269, EBI-6095043;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000305|PubMed:17626015}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17626015}; Cytoplasmic side
CC {ECO:0000305|PubMed:17626015}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8VD37-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VD37-2; Sequence=VSP_020280, VSP_020282, VSP_020284;
CC Name=3;
CC IsoId=Q8VD37-3; Sequence=VSP_020279, VSP_020284, VSP_020285;
CC Name=4;
CC IsoId=Q8VD37-4; Sequence=VSP_020279, VSP_020284;
CC Name=5;
CC IsoId=Q8VD37-5; Sequence=VSP_020281, VSP_020283;
CC Name=6; Synonyms=SGIP1alpha;
CC IsoId=Q8VD37-6; Sequence=VSP_043987, VSP_020285;
CC Name=7;
CC IsoId=Q8VD37-8; Sequence=VSP_020285;
CC -!- TISSUE SPECIFICITY: Detected in brain, spinal cord and cerebellum.
CC {ECO:0000269|PubMed:21747946}.
CC -!- INDUCTION: Up-regulated in the hypothalamus of obese mice.
CC {ECO:0000269|PubMed:15919751}.
CC -!- MISCELLANEOUS: [Isoform 6]: The N-terminal domain (1-97) of this
CC isoform mediates binding to and tubulation of membranes. {ECO:0000305}.
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DR EMBL; AB262964; BAF74784.1; -; mRNA.
DR EMBL; AK014022; BAB29118.1; -; mRNA.
DR EMBL; AK032439; BAC27870.1; -; mRNA.
DR EMBL; AK043018; BAC31435.1; -; mRNA.
DR EMBL; AK148043; BAE28309.1; -; mRNA.
DR EMBL; AK148302; BAE28466.1; -; mRNA.
DR EMBL; BC017596; AAH17596.1; -; mRNA.
DR CCDS; CCDS18404.1; -. [Q8VD37-1]
DR CCDS; CCDS71429.1; -. [Q8VD37-3]
DR CCDS; CCDS71430.1; -. [Q8VD37-4]
DR RefSeq; NP_001272788.1; NM_001285859.1. [Q8VD37-3]
DR RefSeq; NP_001272789.1; NM_001285860.1. [Q8VD37-4]
DR RefSeq; NP_001272791.1; NM_001285862.1.
DR RefSeq; NP_659155.1; NM_144906.2. [Q8VD37-1]
DR RefSeq; XP_006503491.1; XM_006503428.3. [Q8VD37-8]
DR RefSeq; XP_017175890.1; XM_017320401.1.
DR AlphaFoldDB; Q8VD37; -.
DR SMR; Q8VD37; -.
DR BioGRID; 215766; 7.
DR IntAct; Q8VD37; 7.
DR MINT; Q8VD37; -.
DR STRING; 10090.ENSMUSP00000079553; -.
DR iPTMnet; Q8VD37; -.
DR PhosphoSitePlus; Q8VD37; -.
DR SwissPalm; Q8VD37; -.
DR MaxQB; Q8VD37; -.
DR PaxDb; Q8VD37; -.
DR PeptideAtlas; Q8VD37; -.
DR PRIDE; Q8VD37; -.
DR ProteomicsDB; 256980; -. [Q8VD37-1]
DR ProteomicsDB; 256981; -. [Q8VD37-2]
DR ProteomicsDB; 256982; -. [Q8VD37-3]
DR ProteomicsDB; 256983; -. [Q8VD37-4]
DR ProteomicsDB; 256984; -. [Q8VD37-5]
DR ProteomicsDB; 256985; -. [Q8VD37-6]
DR ProteomicsDB; 256986; -. [Q8VD37-8]
DR Antibodypedia; 51610; 80 antibodies from 19 providers.
DR DNASU; 73094; -.
DR Ensembl; ENSMUST00000066824; ENSMUSP00000063712; ENSMUSG00000028524. [Q8VD37-3]
DR Ensembl; ENSMUST00000072481; ENSMUSP00000072301; ENSMUSG00000028524. [Q8VD37-4]
DR Ensembl; ENSMUST00000080728; ENSMUSP00000079553; ENSMUSG00000028524. [Q8VD37-1]
DR Ensembl; ENSMUST00000106882; ENSMUSP00000102495; ENSMUSG00000028524. [Q8VD37-8]
DR Ensembl; ENSMUST00000183855; ENSMUSP00000139337; ENSMUSG00000028524. [Q8VD37-5]
DR GeneID; 73094; -.
DR KEGG; mmu:73094; -.
DR UCSC; uc008two.2; mouse. [Q8VD37-1]
DR UCSC; uc008twq.2; mouse. [Q8VD37-6]
DR UCSC; uc008twr.2; mouse. [Q8VD37-3]
DR UCSC; uc008tws.2; mouse. [Q8VD37-4]
DR UCSC; uc008twt.2; mouse. [Q8VD37-2]
DR CTD; 84251; -.
DR MGI; MGI:1920344; Sgip1.
DR VEuPathDB; HostDB:ENSMUSG00000028524; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000156301; -.
DR HOGENOM; CLU_1673330_0_0_1; -.
DR InParanoid; Q8VD37; -.
DR OMA; NWRCELA; -.
DR TreeFam; TF328986; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 73094; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Sgip1; mouse.
DR PRO; PR:Q8VD37; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VD37; protein.
DR Bgee; ENSMUSG00000028524; Expressed in rostral migratory stream and 186 other tissues.
DR ExpressionAtlas; Q8VD37; baseline and differential.
DR Genevisible; Q8VD37; MM.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; IPI:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:1904000; P:positive regulation of eating behavior; ISO:MGI.
DR GO; GO:2000253; P:positive regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; ISS:UniProtKB.
DR CDD; cd09266; SGIP1_MHD; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Endocytosis; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..806
FT /note="SH3-containing GRB2-like protein 3-interacting
FT protein 1"
FT /id="PRO_0000248396"
FT DOMAIN 537..805
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..545
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 571..573
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 627..806
FT /note="Necessary and sufficient to mediate interaction with
FT CANX"
FT /evidence="ECO:0000269|PubMed:21747946"
FT REGION 645..648
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 791..796
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 33
FT /note="M -> MQGKKKAQKTQLLLTSCFWLRALSLTLSQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17626015"
FT /id="VSP_043987"
FT VAR_SEQ 34
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020279"
FT VAR_SEQ 35..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020280"
FT VAR_SEQ 154..188
FT /note="RKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSK -> VKKLQDPGVPPQL
FT QNLQARSLWMTLWPLLPSLVHH (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020281"
FT VAR_SEQ 154..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020282"
FT VAR_SEQ 189..806
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020283"
FT VAR_SEQ 272..437
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020284"
FT VAR_SEQ 521
FT /note="V -> VENEQPSLVWFDRGKFYLTFE (in isoform 3, isoform 6
FT and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17626015"
FT /id="VSP_020285"
FT CONFLICT 100
FT /note="H -> Q (in Ref. 2; BAC27870)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> H (in Ref. 2; BAE28466)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="T -> P (in Ref. 1; BAF74784)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8VD37-2:243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8VD37-3:274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8VD37-3:338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8VD37-4:274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8VD37-6:533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8VD37-8:505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 806 AA; 86063 MW; 4909A6D1DACCC775 CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEP PYHSKAECAR EGGKKASKKS
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
IKPLQSKDVL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
PTPELTSKKP LDDTLALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPM NPSTESPELA
RPFPTGTPPP LPPKTVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
PKSVAVNTEE KWVHFSDASP EHVTPELTPR EQVVTPPAAS DIPADSPAPA PPGPTGSAGP
PGPPGPRHVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK ECGLGQRATP PPPPPPTYRT
VVSSPGPGSG SGTGTTSGAS SPARPATPLV PCSTTPPPPP PRPPSRPKLP PGKPGVGDVS
RPFSPPIHSS SPPPIAPLAR AESTSSISST NSLSAATTPT VGSSRGPSPL TMGAQDTLPV
AAAFTETVNA YFKGADPSKC IVKITGEMVL SFPAGITRHF ANNPSPAALT FRVVNSSRLE
HVLPNPQLLC CDNTQNDANT KEFWVNMPNL MTHLKKVSEQ KPQATYYNVD MLKYQVSAQG
IQSTPLNLAV NWRCEPASTD LRIDYKYNTD AMSTAVALNN VQFLVPIDGG VTKLQAVLPP
AVWNAEQQRI LWKIPDISQK SENGGVGSLL ARFQLSEGPS KPSPLVVQFT SEGSTLSGCD
IELVGAGYRF SLIKKRFAAG KYLADN
