ID RFIP3_HUMAN STANDARD; PRT; 756 AA. AC O75154; Q9H155; Q9H1G0; Q9NUI0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Rab11 family-interacting protein 3 (Rab11-FIP3) (EF hands-containing DE Rab-interacting protein) (Eferin). GN Name=RAB11FIP3; Synonyms=KIAA0665; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21486406; PubMed=11481332; DOI=10.1074/jbc.M106133200; RA Prekeris R., Davies J.M., Scheller R.H.; RT "Identification of a novel Rab11/25 binding domain present in eferin RT and rip proteins."; RL J. Biol. Chem. 276:38966-38970(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=98403880; PubMed=9734811; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP INTERACTIONS WITH RAB11; RAB11B AND RAB25, AND SUBCELLULAR LOCATION. RX MEDLINE=21486449; PubMed=11495908; DOI=10.1074/jbc.M104831200; RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., RA Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.; RT "Identification and characterization of a family of Rab11-interacting RT proteins."; RL J. Biol. Chem. 276:39067-39075(2001). RN [7] 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). CC -!- SUBUNIT: Forms an heterooligomeric complex with RAB11FIP4. Binds CC to RAB11A, RAB11B and RAB25. CC -!- SUBCELLULAR LOCATION: Colocalizes with RAB11A at recycling CC endosomes. CC -!- SIMILARITY: Contains 2 EF-hand domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF395731; AAL12940.1; -; mRNA. DR EMBL; AB014565; BAA31640.2; ALT_INIT; mRNA. DR EMBL; AE006463; AAK61232.1; -; Genomic_DNA. DR EMBL; AL023881; CAB92745.1; -; Genomic_DNA. DR EMBL; AL049542; CAC17519.1; -; Genomic_DNA. DR EMBL; Z98882; CAC17523.1; -; Genomic_DNA. DR EMBL; BC051360; AAH51360.1; -; mRNA. DR PIR; T00367; T00367. DR Ensembl; ENSG00000090565; Homo sapiens. DR HGNC; HGNC:17224; RAB11FIP3. DR H-InvDB; HIX0012649; -. DR MIM; 608738; -. DR GO; GO:0017137; F:Rab GTPase binding; NAS. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Pfam; PF00036; efhand; 2. DR SMART; SM00054; EFh; 2. DR PROSITE; PS50222; EF_HAND_2; 2. KW Calcium; Repeat. FT DOMAIN 202 237 EF-hand 1. FT DOMAIN 234 269 EF-hand 2. FT CA_BIND 215 226 1 (Potential). FT CA_BIND 247 258 2 (Potential). SQ SEQUENCE 756 AA; 82440 MW; 264CEC399F28AFB9 CRC64; MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP QSPGLDEPAP GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL ASPDAPGPGP RSEAPLPELD PLFSWTEEPE ECGPASCPES APFRLQGSSS SHRARGEVDV FSPFPAPTAG ELALEQGPGS PPQPSDLSQT HPLPSEPVGS QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK DLTKYLDPSG LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV PSECLDAMEE PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE LSPETLCNGQ LGCSDPAFLT PSPTKRLSSK KVARYLHQSG ALTMEALEDP SPELMEGPEE DIADKVVFLE RRVLELEKDT AATGEQHSRL RQENLQLVHR ANALEEQLKE QELRACEMVL EETRRQKELL CKMEREKSIE IENLQTRLQQ LDEENSELRS CTPCLKANIE RLEEEKQKLL DEIESLTLRL SEEQENKRRM GDRLSHERHQ FQRDKEATQE LIEDLRKQLE HLQLLKLEAE QRRGRSSSMG LQEYHSRARE SELEQEVRRL KQDNRNLKEQ NEELNGQIIT LSIQGAKSLF STAFSESLAA EISSVSRDEL MEAIQKQEEI NFRLQDYIDR IIVAIMETNP SILEVK //