VNN1_MOUSE
ID VNN1_MOUSE Reviewed; 512 AA.
AC Q9Z0K8; Q3TJI0; Q8VCT1; Q9DCH8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Pantetheinase;
DE EC=3.5.1.92 {ECO:0000269|PubMed:11042271};
DE AltName: Full=Pantetheine hydrolase;
DE AltName: Full=Vascular non-inflammatory molecule 1;
DE Short=Vanin-1;
DE Flags: Precursor;
GN Name=Vnn1;
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], PROTEIN SEQUENCE OF 24-47, GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8934567; DOI=10.1016/s1074-7613(00)80496-3;
RA Aurrand-Lions M., Galland F., Bazin H., Zakharyev V.M., Imhof B.A.,
RA Naquet P.;
RT "Vanin-1, a novel GPI-linked perivascular molecule involved in thymus
RT homing.";
RL Immunity 5:391-405(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 IDENTIFICATION.
RX PubMed=10567687; DOI=10.1016/s0014-5793(99)01439-8;
RA Maras B., Barra D., Dupre S., Pitari G.;
RT "Is pantetheinase the actual identity of mouse and human vanin-1
RT proteins?";
RL FEBS Lett. 461:149-152(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=11042271; DOI=10.1016/s0014-5793(00)02110-4;
RA Pitari G., Malergue F., Martin F., Philippe J.-M., Massucci M.T.,
RA Chabret C., Maras B., Dupre S., Naquet P., Galland F.;
RT "Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine
RT in tissues of Vanin-1 deficient mice.";
RL FEBS Lett. 483:149-154(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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: Amidohydrolase that hydrolyzes specifically one of the
CC carboamide linkages in D-pantetheine thus recycling pantothenic acid
CC (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:11042271}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine;
CC Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92;
CC Evidence={ECO:0000269|PubMed:11042271};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O95497}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11042271,
CC ECO:0000305|PubMed:8934567}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:11042271, ECO:0000305|PubMed:8934567}.
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level). Ubiquitous.
CC {ECO:0000269|PubMed:11042271}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8934567}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice lack detectable levels
CC of cysteamine in liver and kidney. {ECO:0000269|PubMed:11042271}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000305}.
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DR EMBL; AJ132098; CAA10567.1; -; mRNA.
DR EMBL; AK002773; BAB22347.1; -; mRNA.
DR EMBL; AK145984; BAE26806.1; -; mRNA.
DR EMBL; AK167427; BAE39515.1; -; mRNA.
DR EMBL; CH466540; EDL04771.1; -; Genomic_DNA.
DR EMBL; BC019203; AAH19203.1; -; mRNA.
DR CCDS; CCDS35868.1; -.
DR RefSeq; NP_035834.2; NM_011704.3.
DR AlphaFoldDB; Q9Z0K8; -.
DR SMR; Q9Z0K8; -.
DR STRING; 10090.ENSMUSP00000040599; -.
DR ChEMBL; CHEMBL4802063; -.
DR GlyGen; Q9Z0K8; 4 sites.
DR iPTMnet; Q9Z0K8; -.
DR PhosphoSitePlus; Q9Z0K8; -.
DR CPTAC; non-CPTAC-3504; -.
DR jPOST; Q9Z0K8; -.
DR MaxQB; Q9Z0K8; -.
DR PaxDb; Q9Z0K8; -.
DR PeptideAtlas; Q9Z0K8; -.
DR PRIDE; Q9Z0K8; -.
DR ProteomicsDB; 297608; -.
DR Antibodypedia; 32934; 254 antibodies from 32 providers.
DR DNASU; 22361; -.
DR Ensembl; ENSMUST00000041416; ENSMUSP00000040599; ENSMUSG00000037440.
DR GeneID; 22361; -.
DR KEGG; mmu:22361; -.
DR UCSC; uc007eqc.2; mouse.
DR CTD; 8876; -.
DR MGI; MGI:108395; Vnn1.
DR VEuPathDB; HostDB:ENSMUSG00000037440; -.
DR eggNOG; KOG0806; Eukaryota.
DR GeneTree; ENSGT00390000013823; -.
DR HOGENOM; CLU_033209_2_0_1; -.
DR InParanoid; Q9Z0K8; -.
DR OMA; YEKDWAS; -.
DR OrthoDB; 1276751at2759; -.
DR PhylomeDB; Q9Z0K8; -.
DR TreeFam; TF323645; -.
DR BRENDA; 3.5.1.92; 3474.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-MMU-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 22361; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z0K8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z0K8; protein.
DR Bgee; ENSMUSG00000037440; Expressed in placenta labyrinth and 163 other tissues.
DR Genevisible; Q9Z0K8; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034235; F:GPI anchor binding; TAS:BHF-UCL.
DR GO; GO:0017159; F:pantetheine hydrolase activity; ISS:UniProtKB.
DR GO; GO:0002526; P:acute inflammatory response; IDA:BHF-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0002544; P:chronic inflammatory response; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IMP:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR GO; GO:0015939; P:pantothenate metabolic process; ISS:UniProtKB.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IDA:BHF-UCL.
DR CDD; cd07567; biotinidase_like; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR012101; Biotinidase-like_euk.
DR InterPro; IPR040154; Biotinidase/VNN.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR043957; Vanin_C.
DR PANTHER; PTHR10609; PTHR10609; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF19018; Vanin_C; 1.
DR PIRSF; PIRSF011861; Biotinidase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8934567"
FT CHAIN 24..488
FT /note="Pantetheinase"
FT /id="PRO_0000019714"
FT PROPEP 489..512
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019715"
FT DOMAIN 32..308
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT LIPID 488
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="M -> T (in Ref. 1; CAA10567 and 4; AAH19203)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="S -> G (in Ref. 1; CAA10567)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="KQ -> NE (in Ref. 2; BAB22347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57091 MW; D55E192765A8282C CRC64;
MGMSWWLACA AAFSALCVLK ASSLDTFLAA VYEHAVILPK DTLLPVSHSE ALALMNQNLD
LLEGAIVSAA KQGAHIIVTP EDGIYGVRFT RDTIYPYLEE IPDPQVNWIP CDNPKRFGST
PVQERLSCLA KNNSIYVVAN MGDKKPCNTS DSHCPPDGRF QYNTDVVFDS QGKLVARYHK
QNIFMGEDQF NVPMEPEFVT FDTPFGKFGV FTCFDILFHD PAVTLVTEFQ VDTILFPTAW
MDVLPHLAAI EFHSAWAMGM GVNFLAANLH NPSRRMTGSG IYAPDSPRVF HYDRKTQEGK
LLFAQLKSHP IHSPVNWTSY ASSVESTPTK TQEFQSIVFF DEFTFVELKG IKGNYTVCQN
DLCCHLSYQM SEKRADEVYA FGAFDGLHTV EGQYYLQICI LLKCKTTNLR TCGSSVDTAF
TRFEMFSLSG TFGTRYVFPE VLLSEVKLAP GEFQVSSDGR LVSLKPTSGP VLTIGLFGRL
YGKDWASNAS SDFIAHSLII MLIVTPIIHY LC
