VPS50_MOUSE
ID VPS50_MOUSE Reviewed; 964 AA.
AC Q8CI71; Q6ZPG9; Q7TSR5; Q80XR1; Q8C6D0; Q8C9I6; Q99LN1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Syndetin {ECO:0000250|UniProtKB:Q96JG6};
DE AltName: Full=Bcl2-like protein blm {ECO:0000303|Ref.1};
DE AltName: Full=Coiled-coil domain-containing protein 132 {ECO:0000305};
DE AltName: Full=EARP/GARPII complex subunit VPS50 {ECO:0000250|UniProtKB:Q96JG6};
GN Name=Vps50 {ECO:0000250|UniProtKB:Q96JG6};
GN Synonyms=Ccdc132 {ECO:0000312|MGI:MGI:1920538},
GN Kiaa1861 {ECO:0000303|PubMed:14621295};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Huang H.-Y., Chen S.-Y., Tseng Y.-H., Huang P.-H., Hsu S.-M.;
RT "Identification and characterization of novel members of the bcl-2 family
RT -- blm, expressed specifically in developing embryos.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Thymus, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as component of the EARP complex that is involved in
CC endocytic recycling. The EARP complex associates with Rab4-positive
CC endosomes and promotes recycling of internalized transferrin receptor
CC (TFRC) to the plasma membrane. Within the EARP complex, required to
CC tether the complex to recycling endosomes. Not involved in retrograde
CC transport from early and late endosomes to the trans-Golgi network
CC (TGN). {ECO:0000250|UniProtKB:Q96JG6}.
CC -!- SUBUNIT: Component of the endosome-associated retrograde protein (EARP)
CC complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin (By
CC similarity). The EARP complex interacts with EIPR1 (By similarity).
CC Interacts with VPS51 and VPS53 in an EIPR1-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q96JG6}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome
CC {ECO:0000250|UniProtKB:Q96JG6}. Membrane
CC {ECO:0000250|UniProtKB:F1LSG8}. Note=Associates with membranes in an
CC EIPR1-dependent manner. {ECO:0000250|UniProtKB:F1LSG8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CI71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CI71-2; Sequence=VSP_028661, VSP_028662;
CC Name=3;
CC IsoId=Q8CI71-3; Sequence=VSP_028660, VSP_028663;
CC -!- SIMILARITY: Belongs to the syndetin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY254697; AAO84056.1; -; mRNA.
DR EMBL; AK129458; BAC98268.1; ALT_INIT; mRNA.
DR EMBL; AK042031; BAC31137.1; -; mRNA.
DR EMBL; AK075898; BAC36038.1; -; mRNA.
DR EMBL; BC002304; AAH02304.1; ALT_INIT; mRNA.
DR EMBL; BC036294; AAH36294.2; -; mRNA.
DR EMBL; BC043092; AAH43092.1; -; mRNA.
DR CCDS; CCDS39415.1; -. [Q8CI71-1]
DR CCDS; CCDS51713.1; -. [Q8CI71-2]
DR CCDS; CCDS51714.1; -. [Q8CI71-3]
DR RefSeq; NP_001161222.1; NM_001167750.1. [Q8CI71-2]
DR RefSeq; NP_001161223.1; NM_001167751.1. [Q8CI71-3]
DR RefSeq; NP_077222.4; NM_024260.5. [Q8CI71-1]
DR AlphaFoldDB; Q8CI71; -.
DR SMR; Q8CI71; -.
DR BioGRID; 215896; 5.
DR STRING; 10090.ENSMUSP00000001412; -.
DR iPTMnet; Q8CI71; -.
DR PhosphoSitePlus; Q8CI71; -.
DR SwissPalm; Q8CI71; -.
DR EPD; Q8CI71; -.
DR jPOST; Q8CI71; -.
DR MaxQB; Q8CI71; -.
DR PaxDb; Q8CI71; -.
DR PeptideAtlas; Q8CI71; -.
DR PRIDE; Q8CI71; -.
DR ProteomicsDB; 297817; -. [Q8CI71-1]
DR ProteomicsDB; 297818; -. [Q8CI71-2]
DR ProteomicsDB; 297819; -. [Q8CI71-3]
DR Antibodypedia; 15650; 186 antibodies from 22 providers.
DR Ensembl; ENSMUST00000001412; ENSMUSP00000001412; ENSMUSG00000001376. [Q8CI71-1]
DR Ensembl; ENSMUST00000164052; ENSMUSP00000125872; ENSMUSG00000001376. [Q8CI71-2]
DR Ensembl; ENSMUST00000170873; ENSMUSP00000128323; ENSMUSG00000001376. [Q8CI71-3]
DR GeneID; 73288; -.
DR KEGG; mmu:73288; -.
DR UCSC; uc009avb.2; mouse. [Q8CI71-3]
DR UCSC; uc009avc.2; mouse. [Q8CI71-1]
DR UCSC; uc012ehr.1; mouse. [Q8CI71-2]
DR CTD; 55610; -.
DR MGI; MGI:1920538; Vps50.
DR VEuPathDB; HostDB:ENSMUSG00000001376; -.
DR eggNOG; KOG2939; Eukaryota.
DR GeneTree; ENSGT00390000003442; -.
DR HOGENOM; CLU_009513_1_0_1; -.
DR InParanoid; Q8CI71; -.
DR OMA; MAKVKWD; -.
DR OrthoDB; 293145at2759; -.
DR PhylomeDB; Q8CI71; -.
DR TreeFam; TF106152; -.
DR BioGRID-ORCS; 73288; 4 hits in 41 CRISPR screens.
DR ChiTaRS; Vps50; mouse.
DR PRO; PR:Q8CI71; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CI71; protein.
DR Bgee; ENSMUSG00000001376; Expressed in undifferentiated genital tubercle and 241 other tissues.
DR Genevisible; Q8CI71; MM.
DR GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR019514; Syndetin_C.
DR InterPro; IPR040047; VPS50.
DR InterPro; IPR019515; VPS54_N.
DR PANTHER; PTHR13258; PTHR13258; 1.
DR Pfam; PF10474; DUF2451; 1.
DR Pfam; PF10475; Vps54_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Isopeptide bond;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..964
FT /note="Syndetin"
FT /id="PRO_0000307266"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..107
FT /evidence="ECO:0000255"
FT COILED 216..244
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 963
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT CROSSLNK 963
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96JG6"
FT VAR_SEQ 926..938
FT /note="EYSTKQLTNLVNV -> VRTRVGVLILSGV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028660"
FT VAR_SEQ 926..929
FT /note="EYST -> IFSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028661"
FT VAR_SEQ 930..964
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028662"
FT VAR_SEQ 939..964
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028663"
FT CONFLICT 77..78
FT /note="LP -> PS (in Ref. 3; BAC31137)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..96
FT /note="YRDKLKQQ -> SRYQFKQH (in Ref. 3; BAC31137)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="N -> Y (in Ref. 3; BAC31137)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="F -> S (in Ref. 3; BAC36038)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="V -> M (in Ref. 4; AAH02304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 111174 MW; F88C364742914D0E CRC64;
MQKIKSLMTR QGLKSPPESL NDLGAFESLR VPGKEEFREL REQPSDPQAE QELINSIEQV
YFSADPFDIV KYELEKLPPV LNLQELEEYR DKLKQQQSAV SKKVADLILE KQPAYVKELE
RVTSLQTGLQ LAAVICTNGR RHLNIAKEGF TQASLGLLAN QRKRQLLIGL LKSLRTIKTL
QRTDIRLSEM LEEEDYPGAI QLCLECQKAA STFKHYSCIS ELNSKLQDTL EQIEEQLDVA
LSKICKNFDI NHYTKVQQAY RLLGKTQTAM DQLHMHFTQA IHNTVFQVVL GYVELCAGNT
DTKFQKLQYK DLCTHVTPDS YIPCLADLCK ALWEVMLSYY RTMEWHEKHD NEETAAAAEG
SNVMSTEEAT FDRGYVKKKL EHGLTRIWQD VQLKVKTYLL GTDLSIFKYD DFIFVLDIVS
RLMQVGEEFC GSKSEVLQES IRKQSVNYFK NHHRIRLDEL RMFLENETWE LCPVKSNFSI
LQLHEFKFLE QSRSPSVSPS KQPSATSSKP VTLFEQYCSG GNPFEIQADH KDEETEDVLA
SNGYESDEQE KSAYQDYDSD SDVPEELKRD YVDEQTGDVP VKSVSRETLK SRKKSDYSLN
KVNAPILTNT TLNVIRLVGK YMQMMNILKP IAFDVIHFMS QLFDYYLYAI YTFFGRNDSL
ESTGLGLSSS RLKTTLNRIQ ESLIDLEGSA DPTATLTAAE ERKEKVPSPH LNQLVILTSG
DTLYGLAERV VATESLVFLA EQFEFLQPHL DAVMPAVKKP FLQQFYSQTV STASELRKPI
YWIVAGKAID YEQMLLLMMN VKWDVKEIMS QHNIYVDALL KEFEQFNKRL NEVSKRVRIP
LPVSNILWEH CIRLANRTIV EGYANVKKCS NEGRALMQLD FQQFLMKLEK LTDIRPIPDK
EFVETYIKAY YLTENDMERW IKEHREYSTK QLTNLVNVCL GSHINKKARQ KLLAAIDEID
RPKR
