ID RUFY1_HUMAN Reviewed; 708 AA.
AC Q96T51; Q59FF3; Q71S93; Q9H6I3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=RUN and FYVE domain-containing protein 1;
DE AltName: Full=FYVE-finger protein EIP1;
DE AltName: Full=La-binding protein 1;
DE AltName: Full=Rab4-interacting protein;
DE AltName: Full=Zinc finger FYVE domain-containing protein 12;
GN Name=RUFY1; Synonyms=RABIP4, ZFYVE12;
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] (ISOFORM 1), INTERACTION WITH SSB; RAB4 AND
RP RAB5, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=14617813; DOI=10.1091/mbc.e03-05-0343;
RA Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT "Rabip4' is an effector of rab5 and rab4 and regulates transport through
RT early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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 7-708 (ISOFORM 1), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH BMX, PHOSPHORYLATION AT TYR-389 AND
RP TYR-400, AND MUTAGENESIS OF TYR-389 AND TYR-400.
RX PubMed=11877430; DOI=10.1074/jbc.m111933200;
RA Yang J., Kim O., Wu J., Qiu Y.;
RT "Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain
RT containing protein RUFY1. A possible role of Etk in regulation of vesicle
RT trafficking.";
RL J. Biol. Chem. 277:30219-30226(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-708 (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DOMAIN FYVE-TYPE ZINC-FINGER.
RX PubMed=19296456; DOI=10.1002/prot.22392;
RA He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G.,
RA Kutateladze A.G., Verkhusha V.V., Stahelin R.V., Kutateladze T.G.;
RT "Membrane insertion of the FYVE domain is modulated by pH.";
RL Proteins 76:852-860(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP STRUCTURE BY NMR OF 627-708.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the FYVE domain in zinc finger FYVE domain-
RT containing protein 12.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-267.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol
CC 3-phosphate and participates in early endosomal trafficking.
CC {ECO:0000269|PubMed:14617813}.
CC -!- SUBUNIT: Interacts with BMX. May interact with SSB. Interacts with RAB4
CC and RAB5 that have been activated by GTP-binding.
CC {ECO:0000269|PubMed:11877430, ECO:0000269|PubMed:14617813}.
CC -!- INTERACTION:
CC Q96T51; O75928: PIAS2; NbExp=3; IntAct=EBI-3941207, EBI-348555;
CC Q96T51; Q96DA2: RAB39B; NbExp=4; IntAct=EBI-3941207, EBI-9089467;
CC Q96T51; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-3941207, EBI-747844;
CC Q96T51; Q9BRA2: TXNDC17; NbExp=3; IntAct=EBI-3941207, EBI-1055906;
CC Q96T51; Q68CQ4: UTP25; NbExp=5; IntAct=EBI-3941207, EBI-747711;
CC Q96T51-2; P00973-2: OAS1; NbExp=3; IntAct=EBI-12192715, EBI-12081862;
CC Q96T51-2; Q9H714-3: RUBCNL; NbExp=2; IntAct=EBI-12192715, EBI-9088146;
CC Q96T51-2; Q96T51-2: RUFY1; NbExp=5; IntAct=EBI-12192715, EBI-12192715;
CC Q96T51-2; P36406: TRIM23; NbExp=3; IntAct=EBI-12192715, EBI-740098;
CC Q96T51-2; Q68CQ4: UTP25; NbExp=6; IntAct=EBI-12192715, EBI-747711;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=rabip4';
CC IsoId=Q96T51-1; Sequence=Displayed;
CC Name=2; Synonyms=rabip4;
CC IsoId=Q96T51-2; Sequence=VSP_019785;
CC Name=3;
CC IsoId=Q96T51-3; Sequence=VSP_019786, VSP_019787;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in lung,
CC testis, kidney and brain. {ECO:0000269|PubMed:11877430}.
CC -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions with
CC phosphatidylinositol 3-phosphate in membranes of early endosomes and
CC penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched
CC membranes is substantially increased in acidic conditions.
CC {ECO:0000269|PubMed:19296456}.
CC -!- PTM: Phosphorylation on Tyr-389 and/or Tyr-400 is required for
CC interaction with BMX and endosomal targeting.
CC {ECO:0000269|PubMed:11877430}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK50771.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF312367; AAQ14554.1; -; mRNA.
DR EMBL; AK025904; BAB15276.1; ALT_INIT; mRNA.
DR EMBL; AK075021; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC032571; AAH32571.1; -; mRNA.
DR EMBL; AF361055; AAK50771.1; ALT_FRAME; mRNA.
DR EMBL; AB209507; BAD92744.1; -; mRNA.
DR CCDS; CCDS34312.1; -. [Q96T51-2]
DR CCDS; CCDS4445.2; -. [Q96T51-1]
DR RefSeq; NP_001035541.1; NM_001040451.2. [Q96T51-2]
DR RefSeq; NP_001035542.1; NM_001040452.2. [Q96T51-2]
DR RefSeq; NP_079434.3; NM_025158.4. [Q96T51-1]
DR RefSeq; XP_016865384.1; XM_017009895.1.
DR PDB; 2YQM; NMR; -; A=627-708.
DR PDB; 2YW8; X-ray; 3.00 A; A=627-708.
DR PDBsum; 2YQM; -.
DR PDBsum; 2YW8; -.
DR AlphaFoldDB; Q96T51; -.
DR SMR; Q96T51; -.
DR BioGRID; 123193; 478.
DR IntAct; Q96T51; 47.
DR MINT; Q96T51; -.
DR STRING; 9606.ENSP00000325594; -.
DR GlyGen; Q96T51; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96T51; -.
DR MetOSite; Q96T51; -.
DR PhosphoSitePlus; Q96T51; -.
DR SwissPalm; Q96T51; -.
DR BioMuta; RUFY1; -.
DR DMDM; 110282993; -.
DR EPD; Q96T51; -.
DR jPOST; Q96T51; -.
DR MassIVE; Q96T51; -.
DR MaxQB; Q96T51; -.
DR PaxDb; 9606-ENSP00000325594; -.
DR PeptideAtlas; Q96T51; -.
DR ProteomicsDB; 78184; -. [Q96T51-1]
DR ProteomicsDB; 78185; -. [Q96T51-2]
DR ProteomicsDB; 78186; -. [Q96T51-3]
DR Pumba; Q96T51; -.
DR Antibodypedia; 29480; 253 antibodies from 32 providers.
DR DNASU; 80230; -.
DR Ensembl; ENST00000319449.9; ENSP00000325594.4; ENSG00000176783.15. [Q96T51-1]
DR Ensembl; ENST00000393438.6; ENSP00000377087.2; ENSG00000176783.15. [Q96T51-2]
DR Ensembl; ENST00000437570.6; ENSP00000390025.2; ENSG00000176783.15. [Q96T51-2]
DR Ensembl; ENST00000639102.1; ENSP00000491803.1; ENSG00000284260.2. [Q96T51-2]
DR Ensembl; ENST00000639436.1; ENSP00000491925.1; ENSG00000284260.2. [Q96T51-2]
DR Ensembl; ENST00000639909.2; ENSP00000492748.1; ENSG00000284260.2. [Q96T51-1]
DR GeneID; 80230; -.
DR KEGG; hsa:80230; -.
DR MANE-Select; ENST00000319449.9; ENSP00000325594.4; NM_025158.5; NP_079434.3.
DR UCSC; uc003mka.3; human. [Q96T51-1]
DR AGR; HGNC:19760; -.
DR CTD; 80230; -.
DR DisGeNET; 80230; -.
DR GeneCards; RUFY1; -.
DR HGNC; HGNC:19760; RUFY1.
DR HPA; ENSG00000176783; Low tissue specificity.
DR MIM; 610327; gene.
DR neXtProt; NX_Q96T51; -.
DR OpenTargets; ENSG00000176783; -.
DR PharmGKB; PA134944787; -.
DR VEuPathDB; HostDB:ENSG00000176783; -.
DR eggNOG; KOG1729; Eukaryota.
DR eggNOG; KOG4381; Eukaryota.
DR GeneTree; ENSGT00940000158334; -.
DR HOGENOM; CLU_014576_3_0_1; -.
DR InParanoid; Q96T51; -.
DR OMA; THCKQCK; -.
DR OrthoDB; 5385125at2759; -.
DR PhylomeDB; Q96T51; -.
DR TreeFam; TF323904; -.
DR PathwayCommons; Q96T51; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; Q96T51; -.
DR SIGNOR; Q96T51; -.
DR BioGRID-ORCS; 80230; 12 hits in 1153 CRISPR screens.
DR ChiTaRS; RUFY1; human.
DR EvolutionaryTrace; Q96T51; -.
DR GeneWiki; RUFY1; -.
DR GenomeRNAi; 80230; -.
DR Pharos; Q96T51; Tbio.
DR PRO; PR:Q96T51; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96T51; Protein.
DR Bgee; ENSG00000176783; Expressed in monocyte and 97 other cell types or tissues.
DR ExpressionAtlas; Q96T51; baseline and differential.
DR Genevisible; Q96T51; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IPI:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR CDD; cd15758; FYVE_RUFY1; 1.
DR CDD; cd17694; RUN_RUFY1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.900; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047331; FYVE_RUFY1.
DR InterPro; IPR047335; RUFY1-3.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR047330; RUN_RUFY1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45956:SF4; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45956; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF140741; RUN domain-like; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="RUN and FYVE domain-containing protein 1"
FT /id="PRO_0000097530"
FT DOMAIN 139..271
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT ZN_FING 642..700
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..625
FT /note="Interaction with RAB4"
FT /evidence="ECO:0000250"
FT COILED 321..374
FT /evidence="ECO:0000255"
FT COILED 405..617
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11877430"
FT MOD_RES 400
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11877430"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019785"
FT VAR_SEQ 343..412
FT /note="LSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTKVELETYKQTRQ
FT GLDEMYSDVWKQLKEEKK -> EERMKGQDKGGLSRGRELAASCPAVSLLDTSCLLLAG
FT GGCSALLRLSTAFSCNRPNLLTSRRTAAVKRTK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019786"
FT VAR_SEQ 413..708
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019787"
FT VARIANT 267
FT /note="C -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035985"
FT VARIANT 298
FT /note="H -> Q (in dbSNP:rs6879322)"
FT /id="VAR_051327"
FT MUTAGEN 389
FT /note="Y->F: Abolishes phosphorylation and endosomal
FT targeting; when associated with F-400."
FT /evidence="ECO:0000269|PubMed:11877430"
FT MUTAGEN 400
FT /note="Y->F: Abolishes phosphorylation and endosomal
FT targeting; when associated with F-389."
FT /evidence="ECO:0000269|PubMed:11877430"
FT CONFLICT 519..528
FT /note="SHKLQQELGG -> TTSCSRSWAV (in Ref. 1; AAQ14554)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="D -> N (in Ref. 1; AAQ14554)"
FT /evidence="ECO:0000305"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:2YW8"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:2YQM"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:2YQM"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:2YW8"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:2YQM"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:2YW8"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:2YW8"
FT STRAND 683..687
FT /evidence="ECO:0007829|PDB:2YQM"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:2YW8"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:2YW8"
SQ SEQUENCE 708 AA; 79818 MW; 6697B4BC108AD54F CRC64;
MADREGGCAA GRGRELEPEL EPGPGPGSAL EPGEEFEIVD RSQLPGPGDL RSATRPRAAE
GWSAPILTLA RRATGNLSAS CGSALRAAAG LGGGDSGDGT ARAASKCQMM EERANLMHMM
KLSIKVLLQS ALSLGRSLDA DHAPLQQFFV VMEHCLKHGL KVKKSFIGQN KSFFGPLELV
EKLCPEASDI ATSVRNLPEL KTAVGRGRAW LYLALMQKKL ADYLKVLIDN KHLLSEFYEP
EALMMEEEGM VIVGLLVGLN VLDANLCLKG EDLDSQVGVI DFSLYLKDVQ DLDGGKEHER
ITDVLDQKNY VEELNRHLSC TVGDLQTKID GLEKTNSKLQ EELSAATDRI CSLQEEQQQL
REQNELIRER SEKSVEITKQ DTKVELETYK QTRQGLDEMY SDVWKQLKEE KKVRLELEKE
LELQIGMKTE MEIAMKLLEK DTHEKQDTLV ALRQQLEEVK AINLQMFHKA QNAESSLQQK
NEAITSFEGK TNQVMSSMKQ MEERLQHSER ARQGAEERSH KLQQELGGRI GALQLQLSQL
HEQCSSLEKE LKSEKEQRQA LQRELQHEKD TSSLLRMELQ QVEGLKKELR ELQDEKAELQ
KICEEQEQAL QEMGLHLSQS KLKMEDIKEV NQALKGHAWL KDDEATHCRQ CEKEFSISRR
KHHCRNCGHI FCNTCSSNEL ALPSYPKPVR VCDSCHTLLL QRCSSTAS
//
