EXPH5_MOUSE
ID EXPH5_MOUSE Reviewed; 1960 AA.
AC Q0VAV2; Q3UNV5; Q6A034; Q812E3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Exophilin-5 {ECO:0000312|EMBL:AAI20906.1};
DE AltName: Full=Synaptotagmin-like protein homolog lacking C2 domains b {ECO:0000303|PubMed:11773082};
DE Short=SlaC2-b {ECO:0000303|PubMed:11773082};
DE Short=Slp homolog lacking C2 domains b {ECO:0000303|PubMed:11773082};
GN Name=Exph5 {ECO:0000312|MGI:MGI:2443248};
GN Synonyms=Kiaa0624 {ECO:0000312|EMBL:BAD32262.1},
GN Slac2b {ECO:0000312|MGI:MGI:2443248};
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] {ECO:0000312|EMBL:BAC57424.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAC57424.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:BAC57424.1};
RX PubMed=12590134; DOI=10.1074/jbc.m213090200;
RA Fukuda M.;
RT "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL J. Biol. Chem. 278:15390-15396(2003).
RN [2] {ECO:0000312|EMBL:AAI20906.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAD32262.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1960.
RC TISSUE=Pancreatic islet {ECO:0000312|EMBL:BAD32262.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAE25642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 749-1553.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25642.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:BAE25642.1};
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 [5] {ECO:0000305}
RP INTERACTION WITH RAB27A.
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
CC -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC trafficking. {ECO:0000250|UniProtKB:Q8NEV8}.
CC -!- SUBUNIT: Interacts with RAB27A. {ECO:0000269|PubMed:11773082}.
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DR EMBL; AB098163; BAC57424.1; -; mRNA.
DR EMBL; BC120905; AAI20906.1; -; mRNA.
DR EMBL; AK172984; BAD32262.1; -; mRNA.
DR EMBL; AK143980; BAE25642.1; -; mRNA.
DR CCDS; CCDS23181.1; -.
DR RefSeq; NP_789816.2; NM_176846.3.
DR RefSeq; XP_006510488.1; XM_006510425.3.
DR AlphaFoldDB; Q0VAV2; -.
DR SMR; Q0VAV2; -.
DR BioGRID; 235724; 2.
DR IntAct; Q0VAV2; 1.
DR STRING; 10090.ENSMUSP00000062632; -.
DR iPTMnet; Q0VAV2; -.
DR PhosphoSitePlus; Q0VAV2; -.
DR MaxQB; Q0VAV2; -.
DR PaxDb; Q0VAV2; -.
DR PeptideAtlas; Q0VAV2; -.
DR PRIDE; Q0VAV2; -.
DR ProteomicsDB; 275559; -.
DR Antibodypedia; 54955; 54 antibodies from 15 providers.
DR Ensembl; ENSMUST00000051014; ENSMUSP00000062632; ENSMUSG00000034584.
DR GeneID; 320051; -.
DR KEGG; mmu:320051; -.
DR UCSC; uc009pma.2; mouse.
DR CTD; 23086; -.
DR MGI; MGI:2443248; Exph5.
DR VEuPathDB; HostDB:ENSMUSG00000034584; -.
DR eggNOG; ENOG502RVAY; Eukaryota.
DR GeneTree; ENSGT00390000011087; -.
DR HOGENOM; CLU_001683_0_0_1; -.
DR InParanoid; Q0VAV2; -.
DR OMA; RQNQEEF; -.
DR OrthoDB; 59101at2759; -.
DR PhylomeDB; Q0VAV2; -.
DR TreeFam; TF335662; -.
DR BioGRID-ORCS; 320051; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Exph5; mouse.
DR PRO; PR:Q0VAV2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q0VAV2; protein.
DR Bgee; ENSMUSG00000034584; Expressed in cerebellar cortex and 46 other tissues.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0003334; P:keratinocyte development; ISS:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR InterPro; IPR039916; EXPH5.
DR InterPro; IPR010911; Rab_BD.
DR PANTHER; PTHR21469; PTHR21469; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1960
FT /note="Exophilin-5"
FT /id="PRO_0000355582"
FT DOMAIN 7..63
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT REGION 325..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1906..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT MOD_RES 1819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEV8"
FT CONFLICT 1717
FT /note="A -> V (in Ref. 3; BAD32262)"
FT /evidence="ECO:0000305"
FT CONFLICT 1936
FT /note="V -> D (in Ref. 1; BAC57424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1960 AA; 217643 MW; 9D9864CA1396CB22 CRC64;
MTKVPQGFDF SFLNEEEARK ILQVLERNEE LRRAEKDRIS KLQKTKRDIR WLQGATGEWF
EEIQRKKFCN ETDVNQMLKP PLTYRLQKGM AKNDPMELQT PRSKSLINQK PSVSSRMSFR
SSFASLFSFR RPAKETLKLQ SPRPNRCDER VRPSASVRGT ASAKIYNSPV GNQPVASVFV
PKPAIMREES GMPPPWDASL LESEFFQVLD DLDNKLAQEQ SSGLMNTRVP FNYGSRTQFK
LSHRNSHGHS TGRQQNYHSE TSNMSIYNIL RPGTPREGFK TFSPRTKTIY DMYRTREPRV
LKEDFMQKNA FGSASLCFDS RQRSASPATG SFTARSLHFP ADTQNKSSFT PVRHQQSPKR
TPLSSIIWNR SDASRHRQNQ EESLGVQAPM DIDPEEQYVS PRCFQESRRY EMCHSQNAYQ
SYPLNVPVAN AMSPDTLENS ENMPFYRQSN PFARSFFSST FRQSREQRFG QNSFWSRQEE
YSSWSDFPQS RGPFPSSDKD FEMFSVEANR APSVCSQGVP SQHWRSHSSG HGTYVFRGRE
DSHCWRSDFQ TSPLESMDTS HVNENQHPPH FVTPVGFSIT DSSCHLQSSR LDSQQGYFPV
EEAVDEDPYL CGKAQTPASS FRTPFPLSPD DGRESQSSSF PDSTATLQKI IPNKPDFLPI
RNCTEVPVAC SHSTDSLSLT DTQPNIPVTE TNSEKDMDVS VSKDEQLNKT GQKSRPTGLP
QYVLHTVISN DLPDFQNAHS RDSAQNDRYG FNAPATERSR RSPRVFSRKG TSQIHTTQRD
QSNKLSKNKC FGGDRTLDSA ASPPFIQESG TATSLPSPNQ GCHQKTGSNE ESSNTIKNSH
WCFESTANQK SQPSREPALL DLEQSLSTHS TNDSKLAPGH SISRAPLHVA SDAPQESFLD
ARLVPSTTVF SRSLSDQDPG QEQREEKDKA TKSQDNQLAV NSTDNQESHD SPALPHDAVH
CHPYSPFKNG RGKGRVRRRV SCIEKLTKTE RAAAPTREGS GCAEDQRSIK DPELSTVYCT
LPRKPASFLI HSRQQESKGT VASVRNGPLP FQIKNKAEVP TGKSTSDKPS SPESVSDAAN
AVSGTPKATK KMTDMKAIRS ASVRKGPLPF LIKRAISCPS GEPCSLAESD DRQKSSVLGM
DASPVIPRPG GRIFNSLEGE PSFRESAFSE KELAQEHTGK DRELRAPRMG LFNPSKKTPE
RLCATGSGKE SGRALHKFKT TSMFSVSGDE ENVNCLEVVS IYYTLPRKPS KKFCSLLQQY
TQGTDSLRDA FQGETEALPN ALEIDELNCP AQVQSGIPPP QDPKMQVDSA PCCLSHSPES
KDVSQLPDRE TSKSTLEEMT SVGPDVSLHR EEPTTKEISP SNVSKTAIDD SLSREKREKE
LLRQILRAPL LHQEKGAGKE HTKSHQQPSK GGNSGPSGLP SRSEDNDENS QTRRDSGTCA
GGMASGNGQY PWRDHMAAVV GDRSSRSQPR ETSGTTGSDC QNPTDKMLSD SESQAFALTP
ALCKLQLAEE AQPGGAGLQS EASQAGSQET NTAEMRKVED EEHMLTRDQT LLPRGNNKNK
TNTDETKDRY SGKHRLAAIS KASKRIPAKD LSPRKHVATI FSQSESESGF RRLSLYRPED
NPLSPEPTVK ATESTDESSQ MNVDKSETLL QETTVSSPGP PGQPCHQKSA SILQPHLNGS
PGVLETPPKS EGSKTQISGE LGAPAQLTLT SPLEKGAGHQ QRLSPPFPLE PTQKSTINSH
CQLRHRSAPS PESEPEPHLY RSKSLKNFNV QSDLLCASHP PKARGRHFSE NTSIDNALSQ
LSLEDGSFPN SGYNRRFKSS SELPASYESE SWTSYSNRTR GPKSTSSISR PIDYGIFGKE
QQLAFLENVK RSLTQGRLWK PSFLKNPGFL KDDVLNASNL SQSELVNSPA GQAPEDGVFP
SEPLNIYKDD PVEPLVSDWD TDTTTDDEYY LDEKDKESEL
