ID   IGLL1_MOUSE             Reviewed;         209 AA.
AC   P20764; E9QMX0; Q5W1K3;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Immunoglobulin lambda-like polypeptide 1;
DE   AltName: Full=CD179 antigen-like family member B;
DE   AltName: Full=Ig lambda-5;
DE   AltName: CD_antigen=CD179b;
DE   Flags: Precursor;
GN   Name=Igll1; Synonyms=Igl-5;
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].
RC   STRAIN=129;
RX   PubMed=15950724; DOI=10.1016/j.molimm.2005.01.003;
RA   Minaee S., Farmer D., Georgiou A., Sabbattini P., Webster Z., Chow C.-M.,
RA   Dillon N.;
RT   "Mapping and functional analysis of regulatory sequences in the mouse
RT   lambda5-VpreB1 domain.";
RL   Mol. Immunol. 42:1283-1292(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 105-209, AND TISSUE SPECIFICITY.
RX   PubMed=3024017; DOI=10.1038/324579a0;
RA   Sakaguchi N., Melchers F.;
RT   "Lambda 5, a new light-chain-related locus selectively expressed in pre-B
RT   lymphocytes.";
RL   Nature 324:579-582(1986).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SYVN1.
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: Critical for B-cell development.
CC       {ECO:0000250|UniProtKB:P15814}.
CC   -!- SUBUNIT: Interacts with VPREB1A (By similarity). Interacts with
CC       SYNV1/HRD1 (via N-terminus); this interaction leads to increased IGLL1
CC       ubiquitination and degradation in pre-B cells, possibly through a
CC       lysosomal, not proteasomal, pathway (PubMed:29907570). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P15814, ECO:0000269|PubMed:29907570}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:29907570}. Secreted {ECO:0000250}. Note=In pre-B
CC       cells, localizes predominantly to the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:29907570}.
CC   -!- TISSUE SPECIFICITY: Selectively expressed in pre-B lymphocytes.
CC       {ECO:0000269|PubMed:3024017}.
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DR   EMBL; AJ852426; CAH68524.1; -; Genomic_DNA.
DR   EMBL; AC166832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M30387; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS49775.1; -.
DR   PIR; B26434; B26434.
DR   RefSeq; NP_001177254.1; NM_001190325.1.
DR   AlphaFoldDB; P20764; -.
DR   EMDB; EMD-40456; -.
DR   EMDB; EMD-40457; -.
DR   EMDB; EMD-40467; -.
DR   SMR; P20764; -.
DR   BioGRID; 200596; 3.
DR   FunCoup; P20764; 314.
DR   STRING; 10090.ENSMUSP00000097713; -.
DR   PhosphoSitePlus; P20764; -.
DR   PaxDb; 10090-ENSMUSP00000097713; -.
DR   ProteomicsDB; 269386; -.
DR   Ensembl; ENSMUST00000100136.4; ENSMUSP00000097713.4; ENSMUSG00000075370.13.
DR   GeneID; 16136; -.
DR   KEGG; mmu:16136; -.
DR   UCSC; uc007yje.1; mouse.
DR   AGR; MGI:96529; -.
DR   CTD; 3543; -.
DR   MGI; MGI:96529; Igll1.
DR   VEuPathDB; HostDB:ENSMUSG00000075370; -.
DR   eggNOG; ENOG502SS4M; Eukaryota.
DR   GeneTree; ENSGT00940000164874; -.
DR   InParanoid; P20764; -.
DR   OMA; WGRFPLQ; -.
DR   OrthoDB; 9049585at2759; -.
DR   PhylomeDB; P20764; -.
DR   Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR   Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-MMU-2029481; FCGR activation.
DR   Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR   Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
DR   Reactome; R-MMU-977606; Regulation of Complement cascade.
DR   Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   BioGRID-ORCS; 16136; 5 hits in 76 CRISPR screens.
DR   PRO; PR:P20764; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P20764; protein.
DR   Bgee; ENSMUSG00000075370; Expressed in bone marrow and 17 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; EXP:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISO:GO_Central.
DR   GO; GO:0071735; C:IgG immunoglobulin complex; IBA:GO_Central.
DR   GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR   CDD; cd07699; IgC1_L; 1.
DR   FunFam; 2.60.40.10:FF:000283; Immunoglobulin kappa constant; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR050160; MHC/Immunoglobulin.
DR   PANTHER; PTHR19944:SF98; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Immunoglobulin domain;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..209
FT                   /note="Immunoglobulin lambda-like polypeptide 1"
FT                   /id="PRO_0000153611"
FT   DOMAIN          110..204
FT                   /note="Ig-like C1-type"
FT   REGION          93..104
FT                   /note="J region"
FT                   /evidence="ECO:0000250"
FT   REGION          105..209
FT                   /note="C region"
FT                   /evidence="ECO:0000250"
FT   DISULFID        131..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        208
FT                   /note="Interchain (with a heavy chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        124..129
FT                   /note="ANKATL -> PTRPHV (in Ref. 1; CAH68524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="T -> Q (in Ref. 3; M30387)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="Y -> T (in Ref. 3; M30387)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  22772 MW;  E0ADE721EAEB491E CRC64;
     MKLRVGQTLG TIPRQCEVLL LLLLLGLVDG VHHILSPSSA ERSRAVGPGA SVGSNRPSLW
     ALPGRLLFQI IPRGAGPRCS PHRLPSKPQF WYVFGGGTQL TILGQPKSDP LVTLFLPSLK
     NLQANKATLV CLVSEFYPGT LVVDWKVDGV PVTQGVETTQ PSKQTNNKYM VSSYLTLISD
     QWMPHSRYSC RVTHEGNTVE KSVSPAECS
//