VPREB_HUMAN
ID VPREB_HUMAN Reviewed; 145 AA.
AC P12018; B5MCG2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Immunoglobulin iota chain;
DE AltName: Full=CD179 antigen-like family member A;
DE AltName: Full=Protein VPreB1;
DE AltName: Full=V(pre)B protein;
DE Short=VpreB protein;
DE AltName: CD_antigen=CD179a;
DE Flags: Precursor;
GN Name=VPREB1; Synonyms=VPREB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7935499; DOI=10.1016/0161-5890(94)90105-8;
RA Guelpa-Fonlupt V., Bossy D., Alzari P., Fumoux F., Fougereau M., Schiff C.;
RT "The human pre-B cell receptor: structural constraints for a tentative
RT model of the pseudo-light (psi L) chain.";
RL Mol. Immunol. 31:1099-1108(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
RX PubMed=3258819; DOI=10.1002/j.1460-2075.1988.tb02789.x;
RA Bauer S.R., Kudo A., Melchers F.;
RT "Structure and pre-B lymphocyte restricted expression of the VpreB in
RT humans and conservation of its structure in other mammalian species.";
RL EMBO J. 7:111-116(1988).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-119 IN COMPLEX WITH IGLL1,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=17431183; DOI=10.1126/science.1139412;
RA Bankovich A.J., Raunser S., Juo Z.S., Walz T., Davis M.M., Garcia K.C.;
RT "Structural insight into pre-B cell receptor function.";
RL Science 316:291-294(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 95-108, AND DISULFIDE BOND.
RX PubMed=18287279; DOI=10.1110/ps.073269808;
RA Morstadt L., Bohm A., Yuksel D., Kumar K., Stollar B.D., Baleja J.D.;
RT "Engineering and characterization of a single chain surrogate light chain
RT variable domain.";
RL Protein Sci. 17:458-465(2008).
CC -!- FUNCTION: Associates with the Ig-mu chain to form a molecular complex
CC that is expressed on the surface of pre-B-cells. This complex
CC presumably regulates Ig gene rearrangements in the early steps of B-
CC cell differentiation.
CC -!- SUBUNIT: Interacts with IGLL1 (PubMed:17431183). Interacts with
CC SYNV1/HRD1 (via N-terminus); this interaction leads to increased VPREB1
CC ubiquitination and degradation in pre-B cells, possibly through a
CC lysosomal, not proteasomal, pathway (By similarity).
CC {ECO:0000250|UniProtKB:P13372, ECO:0000269|PubMed:17431183}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P13372}.
CC -!- TISSUE SPECIFICITY: Only expressed by pre-B-cells.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=VPREB1;
CC URL="https://en.wikipedia.org/wiki/VPREB1";
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DR EMBL; S74019; AAB32118.1; -; Genomic_DNA.
DR EMBL; D86992; BAA19987.1; -; Genomic_DNA.
DR EMBL; D88270; BAA20030.1; -; Genomic_DNA.
DR EMBL; CR456609; CAG30495.1; -; mRNA.
DR EMBL; CH471095; EAW59498.1; -; Genomic_DNA.
DR EMBL; M34927; AAA61292.1; -; Genomic_DNA.
DR CCDS; CCDS13798.1; -.
DR PIR; I57832; I57832.
DR PIR; S00258; S00258.
DR RefSeq; NP_009059.1; NM_007128.3.
DR PDB; 2H32; X-ray; 2.70 A; A=20-145.
DR PDB; 2H3N; X-ray; 2.30 A; A/C=21-119.
DR PDB; 3BJ9; X-ray; 2.00 A; 1=22-121.
DR PDBsum; 2H32; -.
DR PDBsum; 2H3N; -.
DR PDBsum; 3BJ9; -.
DR AlphaFoldDB; P12018; -.
DR SMR; P12018; -.
DR BioGRID; 113280; 1.
DR CORUM; P12018; -.
DR IntAct; P12018; 1.
DR STRING; 9606.ENSP00000385361; -.
DR iPTMnet; P12018; -.
DR PhosphoSitePlus; P12018; -.
DR BioMuta; VPREB1; -.
DR DMDM; 9911096; -.
DR PaxDb; P12018; -.
DR PeptideAtlas; P12018; -.
DR PRIDE; P12018; -.
DR ProteomicsDB; 52817; -.
DR TopDownProteomics; P12018; -.
DR Antibodypedia; 23612; 175 antibodies from 26 providers.
DR DNASU; 7441; -.
DR Ensembl; ENST00000403807.4; ENSP00000385361.3; ENSG00000169575.5.
DR GeneID; 7441; -.
DR KEGG; hsa:7441; -.
DR MANE-Select; ENST00000403807.4; ENSP00000385361.3; NM_007128.4; NP_009059.1.
DR UCSC; uc002zvx.2; human.
DR CTD; 7441; -.
DR DisGeNET; 7441; -.
DR GeneCards; VPREB1; -.
DR HGNC; HGNC:12709; VPREB1.
DR HPA; ENSG00000169575; Tissue enriched (bone).
DR MIM; 605141; gene.
DR neXtProt; NX_P12018; -.
DR OpenTargets; ENSG00000169575; -.
DR PharmGKB; PA37324; -.
DR VEuPathDB; HostDB:ENSG00000169575; -.
DR eggNOG; ENOG502RTXJ; Eukaryota.
DR GeneTree; ENSGT00940000161017; -.
DR HOGENOM; CLU_077975_4_0_1; -.
DR InParanoid; P12018; -.
DR OMA; VYSIYWY; -.
DR OrthoDB; 1507021at2759; -.
DR PhylomeDB; P12018; -.
DR TreeFam; TF352061; -.
DR PathwayCommons; P12018; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P12018; -.
DR BioGRID-ORCS; 7441; 15 hits in 1059 CRISPR screens.
DR EvolutionaryTrace; P12018; -.
DR GeneWiki; VPREB1; -.
DR GenomeRNAi; 7441; -.
DR Pharos; P12018; Tbio.
DR PRO; PR:P12018; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P12018; protein.
DR Bgee; ENSG00000169575; Expressed in bone marrow and 24 other tissues.
DR ExpressionAtlas; P12018; baseline and differential.
DR Genevisible; P12018; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Immunoglobulin domain;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..145
FT /note="Immunoglobulin iota chain"
FT /id="PRO_0000015000"
FT DOMAIN 20..132
FT /note="Ig-like V-type"
FT REGION 20..41
FT /note="Framework-1"
FT REGION 42..56
FT /note="Complementarity-determining-1"
FT REGION 57..70
FT /note="Framework-2"
FT REGION 71..81
FT /note="Complementarity-determining-2"
FT REGION 82..115
FT /note="Framework-3"
FT REGION 121..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17431183, ECO:0000269|PubMed:18287279"
FT VARIANT 76
FT /note="D -> N (in dbSNP:rs1320)"
FT /id="VAR_024503"
FT VARIANT 122
FT /note="S -> L (in dbSNP:rs11089979)"
FT /id="VAR_029133"
FT VARIANT 132
FT /note="E -> K (in dbSNP:rs5995720)"
FT /id="VAR_029134"
FT CONFLICT 10
FT /note="L -> H (in Ref. 6; AAA61292)"
FT /evidence="ECO:0000305"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2H32"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3BJ9"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3BJ9"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3BJ9"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3BJ9"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3BJ9"
SQ SEQUENCE 145 AA; 16605 MW; 197665B13AF64D46 CRC64;
MSWAPVLLML FVYCTGCGPQ PVLHQPPAMS SALGTTIRLT CTLRNDHDIG VYSVYWYQQR
PGHPPRFLLR YFSQSDKSQG PQVPPRFSGS KDVARNRGYL SISELQPEDE AMYYCAMGAR
SSEKEERERE WEEEMEPTAA RTRVP
