TRIM9_MOUSE
ID TRIM9_MOUSE Reviewed; 817 AA.
AC Q8C7M3; Q6ZQE5; Q80WT6; Q8C7Z4; Q8CC32; Q8CEG2; Q99PQ3;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM9;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9C026};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM9 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 9;
GN Name=Trim9; Synonyms=Kiaa0282;
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Diencephalon, Head, and Hippocampus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 317-679 (ISOFORM 5).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11960705; DOI=10.1016/s0925-4773(02)00013-8;
RA Berti C., Messali S., Ballabio A., Reymond A., Meroni G.;
RT "TRIM9 is specifically expressed in the embryonic and adult nervous
RT system.";
RL Mech. Dev. 113:159-162(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41; SER-44; SER-46; SER-49
RP AND SER-53, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20085810; DOI=10.1016/j.nbd.2010.01.007;
RA Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K.;
RT "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the
RT brain of Parkinson's disease and dementia with Lewy bodies.";
RL Neurobiol. Dis. 38:210-218(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in
CC cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting
CC signal for proteasomal degradation. May play a role in regulation of
CC neuronal functions. May act as a regulator of synaptic vesicle
CC exocytosis by controlling the availability of SNAP25 for the SNARE
CC complex formation. {ECO:0000250|UniProtKB:Q9C026}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9C026};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9C026}.
CC -!- SUBUNIT: Interacts with SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20085810}. Cell
CC projection, dendrite {ECO:0000269|PubMed:20085810}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000250|UniProtKB:Q91ZY8}. Synapse {ECO:0000250|UniProtKB:Q91ZY8}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZY8}. Note=Enriched
CC at synaptic terminals where it exists in a soluble form and a synaptic
CC vesicle-associated form. Associated with the cytoskeleton (By
CC similarity). Found in proximal dendrites of pyramidal neurons in the
CC cerebral cortex and hippocampus, and Purkinje cells in the cerebellum
CC (PubMed:20085810). {ECO:0000250|UniProtKB:Q91ZY8,
CC ECO:0000269|PubMed:20085810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8C7M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C7M3-2; Sequence=VSP_007930, VSP_007935;
CC Name=3;
CC IsoId=Q8C7M3-3; Sequence=VSP_007931, VSP_007935, VSP_007936;
CC Name=4;
CC IsoId=Q8C7M3-4; Sequence=VSP_007937, VSP_007938;
CC Name=5;
CC IsoId=Q8C7M3-5; Sequence=VSP_007932;
CC Name=6;
CC IsoId=Q8C7M3-6; Sequence=VSP_007933, VSP_007934;
CC -!- TISSUE SPECIFICITY: Brain. Expression is higher in the cerebral cortex
CC and hippocampus (at protein level). Its expression is mainly confined
CC to the central nervous system. The developing neocortex, the dorsal
CC thalamus, the midbrain, the basal area of the hindbrain and spinal cord
CC show high level of expression during embryogenesis. In adult brain, it
CC is detected in the Purkinje cells of the cerebellum, in the
CC hippocampus, and in the cortex. {ECO:0000269|PubMed:11960705,
CC ECO:0000269|PubMed:20085810}.
CC -!- DEVELOPMENTAL STAGE: First seen at 9.5 dpc. From 9.5 dpc to 11.5 dpc,
CC it remains uniformly present in the ventral part of the entire
CC neuroepithelium and in the dorsal root ganglia. A more restricted
CC central nervous system (CNS) expression is observed at 13.5 dpc and
CC 15.5 dpc when it is present in specific regions of the forebrain,
CC midbrain, hindbrain and spinal cord. {ECO:0000269|PubMed:11960705}.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with the N-
CC terminal t-SNARE domain of SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9C026}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be due to an intron retention.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site and to an exon skipping. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice site
CC and ?. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to exon skipping. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be due to an exon inclusion.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK049907; BAC33982.1; -; mRNA.
DR EMBL; AK034029; BAC28552.1; -; mRNA.
DR EMBL; AK028280; BAC25854.1; -; mRNA.
DR EMBL; AK048875; BAC33479.1; -; mRNA.
DR EMBL; AK129109; BAC97919.1; ALT_INIT; mRNA.
DR EMBL; BC052034; AAH52034.1; -; mRNA.
DR EMBL; AF220039; AAG53493.1; -; mRNA.
DR CCDS; CCDS49077.1; -. [Q8C7M3-3]
DR CCDS; CCDS88348.1; -. [Q8C7M3-6]
DR RefSeq; NP_001103672.1; NM_001110202.1. [Q8C7M3-3]
DR RefSeq; NP_001103673.1; NM_001110203.1.
DR RefSeq; NP_001273315.1; NM_001286386.1. [Q8C7M3-6]
DR RefSeq; NP_001273316.1; NM_001286387.1.
DR RefSeq; NP_001273317.1; NM_001286388.1.
DR RefSeq; NP_444397.2; NM_053167.3.
DR AlphaFoldDB; Q8C7M3; -.
DR SMR; Q8C7M3; -.
DR BioGRID; 220445; 10.
DR IntAct; Q8C7M3; 1.
DR MINT; Q8C7M3; -.
DR STRING; 10090.ENSMUSP00000106151; -.
DR iPTMnet; Q8C7M3; -.
DR PhosphoSitePlus; Q8C7M3; -.
DR MaxQB; Q8C7M3; -.
DR PaxDb; Q8C7M3; -.
DR PeptideAtlas; Q8C7M3; -.
DR PRIDE; Q8C7M3; -.
DR ProteomicsDB; 298306; -. [Q8C7M3-1]
DR ProteomicsDB; 298307; -. [Q8C7M3-2]
DR ProteomicsDB; 298308; -. [Q8C7M3-3]
DR ProteomicsDB; 298309; -. [Q8C7M3-4]
DR ProteomicsDB; 298310; -. [Q8C7M3-5]
DR ProteomicsDB; 298311; -. [Q8C7M3-6]
DR Antibodypedia; 10667; 505 antibodies from 25 providers.
DR DNASU; 94090; -.
DR Ensembl; ENSMUST00000110520; ENSMUSP00000106149; ENSMUSG00000021071. [Q8C7M3-3]
DR Ensembl; ENSMUST00000221041; ENSMUSP00000152496; ENSMUSG00000021071. [Q8C7M3-4]
DR Ensembl; ENSMUST00000221370; ENSMUSP00000152692; ENSMUSG00000021071. [Q8C7M3-6]
DR Ensembl; ENSMUST00000222316; ENSMUSP00000152147; ENSMUSG00000021071. [Q8C7M3-1]
DR GeneID; 94090; -.
DR KEGG; mmu:94090; -.
DR UCSC; uc007ntp.3; mouse. [Q8C7M3-1]
DR UCSC; uc007nts.2; mouse. [Q8C7M3-2]
DR UCSC; uc011ynj.2; mouse. [Q8C7M3-3]
DR UCSC; uc011ynl.1; mouse. [Q8C7M3-6]
DR CTD; 114088; -.
DR MGI; MGI:2137354; Trim9.
DR VEuPathDB; HostDB:ENSMUSG00000021071; -.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00940000154071; -.
DR HOGENOM; CLU_013137_19_2_1; -.
DR InParanoid; Q8C7M3; -.
DR OrthoDB; 516512at2759; -.
DR PhylomeDB; Q8C7M3; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94090; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trim9; mouse.
DR PRO; PR:Q8C7M3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C7M3; protein.
DR Bgee; ENSMUSG00000021071; Expressed in piriform cortex and 160 other tissues.
DR ExpressionAtlas; Q8C7M3; baseline and differential.
DR Genevisible; Q8C7M3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..817
FT /note="E3 ubiquitin-protein ligase TRIM9"
FT /id="PRO_0000056209"
FT DOMAIN 374..432
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 440..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 613..794
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 10..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 163..212
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 224..266
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 535..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 273..340
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 535..630
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_007932"
FT VAR_SEQ 535..608
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007931"
FT VAR_SEQ 535..536
FT /note="AA -> GR (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007933"
FT VAR_SEQ 535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007930"
FT VAR_SEQ 537..817
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007934"
FT VAR_SEQ 546..565
FT /note="DTDSEEQTLPFPVPSERLPL -> GMCGWRQSILRLLGIVLLVD (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007937"
FT VAR_SEQ 566..817
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007938"
FT VAR_SEQ 714..732
FT /note="MYVDNNRSWFMHNNSHTNR -> I (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007935"
FT VAR_SEQ 788..817
FT /note="SLWAPGLRACSGCYFKVCPGAVKSPQAPAP -> TLHTGLPVPDFYSSRASI
FT A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007936"
FT CONFLICT 27
FT /note="H -> D (in Ref. 1; BAC28552)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="Q -> H (in Ref. 1; BAC33982)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> Q (in Ref. 1; BAC33982)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> R (in Ref. 4; AAG53493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 90870 MW; F23A355F6FF5762D CRC64;
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSR RASGSGVSDY
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPP THLSPALAPV
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRT
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV AADGYILELD
DGSGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEAAGAHE
TKPMKDTDSE EQTLPFPVPS ERLPLRRMSP FSSTLNLQPS FPGRSYFDFR SSPHQLSLHS
SLQSLNAPGC NFETQSASYS QLVDIKKLLA VAWFAFDPGS AHSDIIFSND NLTVTCSSYD
DRVVLGKTGF SKGVHYWELT IDRYDNHPDP AFGVARIDVM KDMMLGKDDK AWAMYVDNNR
SWFMHNNSHT NRTEGGITKG ATIGVLLDLN RKTLTFFVNN EQQGPIAFEN VEGLFFPAVS
LNRNVQVSLW APGLRACSGC YFKVCPGAVK SPQAPAP
