ID   RFIP5_HUMAN             Reviewed;         653 AA.
AC   Q9BXF6; O94939; Q9P0M1;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-DEC-2008, entry version 61.
DE   RecName: Full=Rab11 family-interacting protein 5;
DE            Short=Rab11-FIP5;
DE   AltName: Full=Rab11-interacting protein Rip11;
DE   AltName: Full=Gamma-SNAP-associated factor 1;
DE            Short=Gaf-1;
DE   AltName: Full=Phosphoprotein pp75;
GN   Name=RAB11FIP5; Synonyms=GAF1, KIAA0857, RIP11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB11A, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=21111052; PubMed=11163216; DOI=10.1016/S1097-2765(00)00140-4;
RA   Prekeris R., Klumperman J., Scheller R.H.;
RT   "A Rab11/Rip11 protein complex regulates apical membrane trafficking
RT   via recycling endosomes.";
RL   Mol. Cell 6:1437-1448(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=99156230; PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 105-653, INTERACTION WITH SSA2, DISEASE,
RP   TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC   TISSUE=Keratinocyte;
RX   MEDLINE=20015020; PubMed=10545525;
RA   Wang D., Buyon J.P., Zhu W., Chan E.K.L.;
RT   "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and
RT   identification of distinct human autoantibodies.";
RL   J. Clin. Invest. 104:1265-1275(1999).
RN   [5]
RP   INTERACTION WITH NAPG, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21201156; PubMed=11278501; DOI=10.1074/jbc.M009424200;
RA   Chen D., Xu W., He P., Medrano E.E., Whiteheart S.W.;
RT   "Gaf-1, a gamma-SNAP-binding protein associated with the
RT   mitochondria.";
RL   J. Biol. Chem. 276:13127-13135(2001).
RN   [6]
RP   SUBUNIT.
RX   MEDLINE=22358406; PubMed=12470645; DOI=10.1016/S0006-291X(02)02720-1;
RA   Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.;
RT   "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its
RT   overexpression condenses the Rab11 positive compartment in HeLa
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 299:770-779(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=15144186; DOI=10.1021/ac035352d;
RA   Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA   Peters E.C.;
RT   "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT   from human T cells using immobilized metal affinity chromatography and
RT   tandem mass spectrometry.";
RL   Anal. Chem. 76:2763-2772(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-538, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Rab effector involved in protein trafficking from apical
CC       recycling endosomes to the apical plasma membrane.
CC   -!- SUBUNIT: Forms an heterooligomeric complex with RAB11FIP4. Binds
CC       NAPG and SSA2. Binds RAB11A that has been activated by GTP
CC       binding.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane;
CC       Peripheral membrane protein. Mitochondrion membrane; Peripheral
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected at low levels in heart, brain,
CC       placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle
CC       and pancreas.
CC   -!- DOMAIN: Binds to vesicles enriched in neutral phospholipids via
CC       its C2 domain. The interaction is favored by Mg(2+) rather than
CC       Ca(2+).
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC   -!- DISEASE: Antibodies against RIP11 are found in sera from patients
CC       with systemic lupus erythematosus (SLE) or Sjoegren syndrome (SS),
CC       and in the sera from mothers of children with neonatal lupus
CC       erythematosus (NLE).
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; AF334812; AAK20892.1; -; mRNA.
DR   EMBL; AB020664; BAA74880.1; ALT_INIT; mRNA.
DR   EMBL; BC035013; AAH35013.1; -; mRNA.
DR   EMBL; AF153085; AAF34356.1; -; mRNA.
DR   PIR; T17312; T17312.
DR   RefSeq; NP_056285.1; -.
DR   UniGene; Hs.24557; -.
DR   IntAct; Q9BXF6; 3.
DR   PhosphoSite; Q9BXF6; -.
DR   PRIDE; Q9BXF6; -.
DR   Ensembl; ENSG00000135631; Homo sapiens.
DR   GeneID; 26056; -.
DR   KEGG; hsa:26056; -.
DR   GeneCards; GC02M073212; -.
DR   H-InvDB; HIX0002158; -.
DR   HGNC; HGNC:24845; RAB11FIP5.
DR   MIM; 605536; gene.
DR   PharmGKB; PA134971129; -.
DR   HOVERGEN; Q9BXF6; -.
DR   NextBio; 47930; -.
DR   ArrayExpress; Q9BXF6; -.
DR   CleanEx; HS_RAB11FIP5; -.
DR   GermOnline; ENSG00000135631; Homo sapiens.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Membrane; Mitochondrion; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    653       Rab11 family-interacting protein 5.
FT                                /FTId=PRO_0000097307.
FT   DOMAIN        6    128       C2.
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     306    306       Phosphotyrosine (By similarity).
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     538    538       Phosphoserine.
FT   CONFLICT    176    176       Missing (in Ref. 3; AAH35013).
FT   CONFLICT    503    503       E -> G (in Ref. 3; AAH35013).
FT   CONFLICT    599    599       H -> N (in Ref. 3; AAH35013).
SQ   SEQUENCE   653 AA;  70415 MW;  716725537AA9D86E CRC64;
     MALVRGAEPA AGPSRWLPTH VQVTVLRARG LRGKSSGAGS TSDAYTVIQV GREKYSTSVV
     EKTHGCPEWR EECSFELPPG ALDGLLRAQE ADAGPAPWAA SSAAACELVL TTMHRSLIGV
     DKFLGQATVA LDEVFGAGRA QHTQWYKLHS KPGKKEKERG EIEVTIQFTR NNLSASMFDL
     SMKDKPRSPF SKIRDKMKGK KKYDLESASA ILPSSAIEDP DLGSLGKMGK AKGFFLRNKL
     RKSSLTQSNT SLGSDSTLSS ASGSLAYQGP GAELLTRSPS RSSWLSTEGG RDSAQSPKLF
     THKRTYSDEA NQMRVAPPRA LLDLQGHLDA ASRSSLCVNG SHIYNEEPQG PVRHRSSISG
     SLPSSGSLQA VSSRFSEEGP RSTDDTWPRG SRSNSSSEAV LGQEELSAQA KVLAPGASHP
     GEEEGARLPE GKPVQVATPI VASSEAVAEK EGARKEERKP RMGLFHHHHQ GLSRSELGRR
     SSLGEKGGPI LGASPHHSSS GEEKAKSSWF GLREAKDPTQ KPSPHPVKPL SAAPVEGSPD
     RKQSRSSLSI ALSSGLEKLK TVTSGSIQPV TQAPQAGQMV DTKRLKDSAV LDQSAKYYHL
     THDELISLLL QRERELSQRD EHVQELESYI DRLLVRIMET SPTLLQIPPG PPK
//