MCF2L_HUMAN
ID MCF2L_HUMAN Reviewed; 1137 AA.
AC O15068; A2A2X1; A2A2X2; A2A3G6; A2A3G8; B4DHD6; B4DIL6; E9PDN8; Q5JU56;
AC Q5VXT1; Q6ZWD4; Q765G8; Q765G9; Q8N679;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Guanine nucleotide exchange factor DBS;
DE AltName: Full=DBL's big sister;
DE AltName: Full=MCF2-transforming sequence-like protein;
GN Name=MCF2L; Synonyms=KIAA0362, OST {ECO:0000303|PubMed:15157669};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, DOMAIN, AND INTERACTION WITH CDC42 AND INOSITOL PHOSPHOLIPIDS.
RX PubMed=15157669; DOI=10.1016/j.cellsig.2004.01.007;
RA Ueda S., Kataoka T., Satoh T.;
RT "Role of the Sec14-like domain of Dbl family exchange factors in the
RT regulation of Rho family GTPases in different subcellular sites.";
RL Cell. Signal. 16:899-906(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Muscle;
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).
CC -!- FUNCTION: Guanine nucleotide exchange factor that catalyzes guanine
CC nucleotide exchange on RHOA and CDC42, and thereby contributes to the
CC regulation of RHOA and CDC42 signaling pathways (By similarity). Seems
CC to lack activity with RAC1. Becomes activated and highly tumorigenic by
CC truncation of the N-terminus (By similarity). Isoform 5 activates CDC42
CC (PubMed:15157669). {ECO:0000250|UniProtKB:Q63406,
CC ECO:0000269|PubMed:15157669}.
CC -!- FUNCTION: [Isoform 3]: Does not catalyze guanine nucleotide exchange on
CC CDC42 (PubMed:15157669). {ECO:0000269|PubMed:15157669}.
CC -!- SUBUNIT: Interacts with GTP-bound RAC1 (By similarity). Interacts with
CC CDC42 (PubMed:15157669). Interacts with RHOA. Interacts with CCPG1,
CC which results in specific inhibition of its exchange activity toward
CC RHOA, but does not affect its activity on CDC42 (By similarity).
CC {ECO:0000250|UniProtKB:Q63406, ECO:0000250|UniProtKB:Q64096,
CC ECO:0000269|PubMed:15157669}.
CC -!- INTERACTION:
CC O15068-4; O76024: WFS1; NbExp=3; IntAct=EBI-21375623, EBI-720609;
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000269|PubMed:15157669}. Cell membrane
CC {ECO:0000269|PubMed:15157669}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15157669}; Cytoplasmic side
CC {ECO:0000269|PubMed:15157669}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:15157669}. Endomembrane system
CC {ECO:0000269|PubMed:15157669}. Note=Interaction with membranes enriched
CC in phosphoinositides is mediated by the CRAL-TRIO domain.
CC {ECO:0000269|PubMed:15157669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64096}. Cell
CC membrane {ECO:0000250|UniProtKB:Q64096}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64096}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q64096}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. Experimental confirmation may be lacking for some
CC isoforms.;
CC Name=1;
CC IsoId=O15068-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15068-2; Sequence=VSP_026120, VSP_026128;
CC Name=3; Synonyms=Ost-II {ECO:0000303|PubMed:15157669};
CC IsoId=O15068-3; Sequence=VSP_026121, VSP_026128;
CC Name=4;
CC IsoId=O15068-4; Sequence=VSP_026122, VSP_026126, VSP_026127;
CC Name=5; Synonyms=Ost-I {ECO:0000303|PubMed:15157669};
CC IsoId=O15068-5; Sequence=VSP_026119, VSP_026128;
CC Name=6;
CC IsoId=O15068-6; Sequence=VSP_026123;
CC Name=7;
CC IsoId=O15068-9; Sequence=VSP_026123, VSP_039037;
CC Name=8;
CC IsoId=O15068-8; Sequence=VSP_026124;
CC Name=9;
CC IsoId=O15068-10; Sequence=VSP_026122, VSP_039037;
CC -!- DOMAIN: The CRAL-TRIO domain mediates interaction with various inositol
CC phospholipids, such as phosphatidylinositol 3-phosphate (PI3P),
CC phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-
CC phosphate (PI5P). {ECO:0000269|PubMed:15157669}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250|UniProtKB:Q64096}.
CC -!- SIMILARITY: Belongs to the MCF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20817.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB116074; BAD08351.1; -; mRNA.
DR EMBL; AB116075; BAD08352.1; -; mRNA.
DR EMBL; AB002360; BAA20817.1; ALT_INIT; mRNA.
DR EMBL; AK295047; BAG58097.1; -; mRNA.
DR EMBL; AK295670; BAG58528.1; -; mRNA.
DR EMBL; AL356740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011853; AAH11853.1; -; mRNA.
DR EMBL; BC020208; AAH20208.1; -; mRNA.
DR CCDS; CCDS45070.2; -. [O15068-9]
DR CCDS; CCDS81782.1; -. [O15068-4]
DR CCDS; CCDS9527.3; -. [O15068-10]
DR RefSeq; NP_001106203.2; NM_001112732.2. [O15068-9]
DR RefSeq; NP_001307744.1; NM_001320815.1.
DR RefSeq; NP_001307745.1; NM_001320816.1.
DR RefSeq; NP_001307746.1; NM_001320817.1. [O15068-4]
DR RefSeq; NP_079255.4; NM_024979.4. [O15068-10]
DR AlphaFoldDB; O15068; -.
DR SMR; O15068; -.
DR BioGRID; 116865; 17.
DR IntAct; O15068; 11.
DR MINT; O15068; -.
DR STRING; 9606.ENSP00000440374; -.
DR ChEMBL; CHEMBL4524032; -.
DR SwissLipids; SLP:000001547; -.
DR iPTMnet; O15068; -.
DR PhosphoSitePlus; O15068; -.
DR BioMuta; MCF2L; -.
DR EPD; O15068; -.
DR jPOST; O15068; -.
DR MassIVE; O15068; -.
DR MaxQB; O15068; -.
DR PaxDb; O15068; -.
DR PeptideAtlas; O15068; -.
DR PRIDE; O15068; -.
DR ProteomicsDB; 19715; -.
DR ProteomicsDB; 48418; -. [O15068-1]
DR ProteomicsDB; 48419; -. [O15068-2]
DR ProteomicsDB; 48420; -. [O15068-3]
DR ProteomicsDB; 48421; -. [O15068-4]
DR ProteomicsDB; 48422; -. [O15068-5]
DR ProteomicsDB; 48423; -. [O15068-6]
DR ProteomicsDB; 48424; -. [O15068-8]
DR ProteomicsDB; 48425; -. [O15068-9]
DR Antibodypedia; 1984; 156 antibodies from 32 providers.
DR DNASU; 23263; -.
DR Ensembl; ENST00000375597.8; ENSP00000364747.4; ENSG00000126217.21. [O15068-4]
DR Ensembl; ENST00000375604.6; ENSP00000364754.3; ENSG00000126217.21. [O15068-10]
DR Ensembl; ENST00000375608.7; ENSP00000364758.3; ENSG00000126217.21. [O15068-1]
DR Ensembl; ENST00000397030.5; ENSP00000380225.1; ENSG00000126217.21. [O15068-2]
DR Ensembl; ENST00000421756.5; ENSP00000397285.1; ENSG00000126217.21. [O15068-3]
DR Ensembl; ENST00000535094.7; ENSP00000440374.2; ENSG00000126217.21. [O15068-9]
DR GeneID; 23263; -.
DR KEGG; hsa:23263; -.
DR MANE-Select; ENST00000535094.7; ENSP00000440374.2; NM_001112732.3; NP_001106203.2. [O15068-9]
DR UCSC; uc001vss.5; human. [O15068-1]
DR CTD; 23263; -.
DR DisGeNET; 23263; -.
DR GeneCards; MCF2L; -.
DR HGNC; HGNC:14576; MCF2L.
DR HPA; ENSG00000126217; Tissue enhanced (brain).
DR MIM; 609499; gene.
DR neXtProt; NX_O15068; -.
DR OpenTargets; ENSG00000126217; -.
DR PharmGKB; PA30685; -.
DR VEuPathDB; HostDB:ENSG00000126217; -.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000157874; -.
DR HOGENOM; CLU_007130_1_0_1; -.
DR InParanoid; O15068; -.
DR OMA; LQRICTI; -.
DR OrthoDB; 118479at2759; -.
DR PhylomeDB; O15068; -.
DR TreeFam; TF318080; -.
DR PathwayCommons; O15068; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; O15068; -.
DR SIGNOR; O15068; -.
DR BioGRID-ORCS; 23263; 21 hits in 1074 CRISPR screens.
DR ChiTaRS; MCF2L; human.
DR GeneWiki; MCF2L; -.
DR GenomeRNAi; 23263; -.
DR Pharos; O15068; Tbio.
DR PRO; PR:O15068; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O15068; protein.
DR Bgee; ENSG00000126217; Expressed in right hemisphere of cerebellum and 170 other tissues.
DR ExpressionAtlas; O15068; baseline and differential.
DR Genevisible; O15068; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd01227; PH_Dbs; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11857; SH3_DBS; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035534; DBS_PH.
DR InterPro; IPR035532; DBS_SH3.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00435; Spectrin; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH3 domain.
FT CHAIN 1..1137
FT /note="Guanine nucleotide exchange factor DBS"
FT /id="PRO_0000080935"
FT DOMAIN 52..224
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 351..456
FT /note="Spectrin"
FT DOMAIN 631..811
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 829..945
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1055..1116
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 557..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 503..529
FT /evidence="ECO:0000255"
FT COMPBIAS 601..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63406"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63406"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64096"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64096"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64096"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64096"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64096"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15157669"
FT /id="VSP_026119"
FT VAR_SEQ 1..56
FT /note="MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEAT
FT AMAT -> MPLRGGAGPSPASHGPTHGPSDPRTCLPGRGAGGMRPHGRGALGCCGLCSF
FT YTCHGAAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9205841"
FT /id="VSP_026120"
FT VAR_SEQ 1..56
FT /note="MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEAT
FT AMAT -> MAEKGASRGTLRRLWSLPRRRRGTAGRSRP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15157669"
FT /id="VSP_026121"
FT VAR_SEQ 1..56
FT /note="MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEAT
FT AMAT -> MTVRRLSLLCRDLWALWLLLKAGA (in isoform 4 and isoform
FT 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026122"
FT VAR_SEQ 1..56
FT /note="MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEAT
FT AMAT -> MRFWLRTEEMALEEMVQRLNAVSKHT (in isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026123"
FT VAR_SEQ 1..56
FT /note="MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEAT
FT AMAT -> MGDGKAVRISVAEMKSYYLYSEWCSWLLSVAE (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_026124"
FT VAR_SEQ 1015..1016
FT /note="GW -> EP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026126"
FT VAR_SEQ 1017..1137
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026127"
FT VAR_SEQ 1094..1137
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15157669,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_026128"
FT VAR_SEQ 1128..1137
FT /note="GKAHVPRAHP -> ESSPGSAVLSNSSSCSEGGQAPFSDLQG (in
FT isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039037"
FT CONFLICT 580
FT /note="C -> S (in Ref. 3; BAG58097)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="E -> G (in Ref. 3; BAG58097)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="F -> L (in Ref. 3; BAG58528)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="P -> L (in Ref. 3; BAG58528)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="C -> R (in Ref. 3; BAG58097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1137 AA; 128109 MW; B2830890A69C8377 CRC64;
MFDCWRFILC KRPGSNSYSS PQRPNEAKKE ETDHQIDVSD VIRLVQDTPE ATAMATDEIM
HQDIVPLCAA DIQDQLKKRF AYLSGGRGQD GSPVITFPDY PAFSEIPDKE FQNVMTYLTS
IPSLQDAGIG FILVIDRRRD KWTSVKASVL RIAASFPANL QLVLVLRPTG FFQRTLSDIA
FKFNRDDFKM KVPVIMLSSV PDLHGYIDKS QLTEDLGGTL DYCHSRWLCQ RTAIESFALM
VKQTAQMLQS FGTELAETEL PNDVQSTSSV LCAHTEKKDK AKEDLRLALK EGHSVLESLR
ELQAEGSEPS VNQDQLDNQA TVQRLLAQLN ETEAAFDEFW AKHQQKLEQC LQLRHFEQGF
REVKAILDAA SQKIATFTDI GNSLAHVEHL LRDLASFEEK SGVAVERARA LSLDGEQLIG
NKHYAVDSIR PKCQELRHLC DQFSAEIARR RGLLSKSLEL HRRLETSMKW CDEGIYLLAS
QPVDKCQSQD GAEAALQEIE KFLETGAENK IQELNAIYKE YESILNQDLM EHVRKVFQKQ
ASMEEVFHRR QASLKKLAAR QTRPVQPVAP RPEALAKSPC PSPGIRRGSE NSSSEGGALR
RGPYRRAKSE MSESRQGRGS AGEEEESLAI LRRHVMSELL DTERAYVEEL LCVLEGYAAE
MDNPLMAHLL STGLHNKKDV LFGNMEEIYH FHNRIFLREL ENYTDCPELV GRCFLERMED
FQIYEKYCQN KPRSESLWRQ CSDCPFFQEC QRKLDHKLSL DSYLLKPVQR ITKYQLLLKE
MLKYSRNCEG AEDLQEALSS ILGILKAVND SMHLIAITGY DGNLGDLGKL LMQGSFSVWT
DHKRGHTKVK ELARFKPMQR HLFLHEKAVL FCKKREENGE GYEKAPSYSY KQSLNMAAVG
ITENVKGDAK KFEIWYNARE EVYIVQAPTP EIKAAWVNEI RKVLTSQLQA CREASQHRAL
EQSQSLPLPA PTSTSPSRGN SRNIKKLEER KTDPLSLEGY VSSAPLTKPP EKGKGWSKTS
HSLEAPEDDG GWSSAEEQIN SSDAEEDGGL GPKKLVPGKY TVVADHEKGG PDALRVRSGD
VVELVQEGDE GLWYVRDPTT GKEGWVPASS LSVRLGPSGS AQCLSSSGKA HVPRAHP
