ID   VPREB_MOUSE             Reviewed;         142 AA.
AC   P13372;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Immunoglobulin iota chain;
DE   AltName: Full=Protein VPreB1;
DE   AltName: CD_antigen=CD179a;
DE   Flags: Precursor;
GN   Name=Vpreb1;
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 [GENOMIC DNA / MRNA].
RC   STRAIN=C57BL/6 X DBA/2J;
RX   PubMed=3117530; DOI=10.1002/j.1460-2075.1987.tb02500.x;
RA   Kudo A., Melchers F.;
RT   "A second gene, VpreB in the lambda 5 locus of the mouse, which appears to
RT   be selectively expressed in pre-B lymphocytes.";
RL   EMBO J. 6:2267-2272(1987).
RN   [2]
RP   INTERACTION WITH SYVN1, AND SUBCELLULAR LOCATION.
RX   PubMed=29907570; DOI=10.1074/jbc.ra117.001267;
RA   Yang Y., Kong S., Zhang Y., Melo-Cardenas J., Gao B., Zhang Y., Zhang D.D.,
RA   Zhang B., Song J., Thorp E., Zhang K., Zhang J., Fang D.;
RT   "The endoplasmic reticulum-resident E3 ubiquitin ligase Hrd1 controls a
RT   critical checkpoint in B cell development in mice.";
RL   J. Biol. Chem. 293:12934-12944(2018).
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 (By similarity). 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 (PubMed:29907570).
CC       {ECO:0000250|UniProtKB:P12018, ECO:0000269|PubMed:29907570}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000305|PubMed:29907570}.
CC   -!- TISSUE SPECIFICITY: Only expressed by pre-B-cells.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR   EMBL; X05556; CAA29071.1; -; mRNA.
DR   EMBL; X05557; CAA29072.1; -; Genomic_DNA.
DR   CCDS; CCDS27989.1; -.
DR   PIR; A28344; A28344.
DR   RefSeq; NP_058678.1; NM_016982.2.
DR   AlphaFoldDB; P13372; -.
DR   SMR; P13372; -.
DR   BioGRID; 204532; 1.
DR   STRING; 10090.ENSMUSP00000074537; -.
DR   PhosphoSitePlus; P13372; -.
DR   PaxDb; P13372; -.
DR   PRIDE; P13372; -.
DR   DNASU; 22362; -.
DR   Ensembl; ENSMUST00000075017; ENSMUSP00000074537; ENSMUSG00000059305.
DR   GeneID; 22362; -.
DR   KEGG; mmu:22362; -.
DR   UCSC; uc007yjg.2; mouse.
DR   CTD; 7441; -.
DR   MGI; MGI:98936; Vpreb1.
DR   VEuPathDB; HostDB:ENSMUSG00000059305; -.
DR   eggNOG; ENOG502RTXJ; Eukaryota.
DR   GeneTree; ENSGT00940000161017; -.
DR   HOGENOM; CLU_077975_4_0_1; -.
DR   InParanoid; P13372; -.
DR   OMA; DINMYNI; -.
DR   OrthoDB; 1507021at2759; -.
DR   PhylomeDB; P13372; -.
DR   TreeFam; TF352061; -.
DR   BioGRID-ORCS; 22362; 0 hits in 39 CRISPR screens.
DR   PRO; PR:P13372; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P13372; protein.
DR   Bgee; ENSMUSG00000059305; Expressed in choroid plexus and 60 other tissues.
DR   ExpressionAtlas; P13372; baseline and differential.
DR   Genevisible; P13372; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IPI:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
DR   GO; GO:0001782; P:B cell homeostasis; IGI:MGI.
DR   GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0006955; P:immune response; IPI:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IDA:MGI.
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   Disulfide bond; Endoplasmic reticulum; Immunoglobulin domain;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..142
FT                   /note="Immunoglobulin iota chain"
FT                   /id="PRO_0000015001"
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   DISULFID        41..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   142 AA;  16125 MW;  2E18BF963A0F448C CRC64;
     MAWTSVLLML LAYLTGCGPQ PMVHQPPLAS SSLGATIRLS CTLSNDHNIG IYSIYWYQQR
     PGHPPRFLLR YFSHSDKHQG PDIPPRFSGS KDTTRNLGYL SISELQPEDE AVYYCAVGLR
     SQEKKRMERE WEGEKSYTDL GS