IGHA_MOUSE
ID IGHA_MOUSE Reviewed; 344 AA.
AC P01878;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ig alpha chain C region;
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] (MYELOMAS ABE48 AND J558).
RX PubMed=6790349; DOI=10.1016/0378-1119(81)90016-0;
RA Auffray C., Nageotte R., Sikorav J.-L., Heidmann O., Rougeon F.;
RT "Mouse immunoglobulin A: nucleotide sequence of the structural gene for the
RT alpha heavy chain derived from cloned cDNAs.";
RL Gene 13:365-374(1981).
RN [2]
RP PROTEIN SEQUENCE OF 1-213 (MOPC 47A).
RX PubMed=115869; DOI=10.1016/s0021-9258(19)86502-x;
RA Robinson E.A., Appella E.;
RT "Amino acid sequence of a mouse myeloma immunoglobin heavy chain (MOPC 47
RT A) with a 100-residue deletion.";
RL J. Biol. Chem. 254:11418-11430(1979).
RN [3]
RP PROTEIN SEQUENCE OF 1-254 AND 291-344 (M511), AND GLYCOSYLATION AT ASN-331
RP (VARIANT ASN-331).
RX PubMed=6776528; DOI=10.1073/pnas.77.8.4909;
RA Robinson E.A., Appella E.;
RT "Complete amino acid sequence of a mouse immunoglobulin alpha chain (MOPC
RT 511).";
RL Proc. Natl. Acad. Sci. U.S.A. 77:4909-4913(1980).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
CC -!- FUNCTION: Ig alpha is the major immunoglobulin class in body
CC secretions. It may serve both to defend against local infection and to
CC prevent access of foreign antigens to the general immunologic system.
CC -!- MISCELLANEOUS: The final C-region domain is deleted from PubMed:115869
CC chain. It was isolated from a myeloma protein that contains 1 light and
CC 1 heavy chain per molecule, linked by a disulfide bond. In contrast,
CC normal mouse IgA molecules contain 2 light and 2 heavy chains and lack
CC a light-heavy chain disulfide bond.
CC -!- MISCELLANEOUS: M511 chain was isolated from a myeloma protein that
CC binds phosphorylcholine.
CC -!- MISCELLANEOUS: M511 sequence was compared with that of mouse MOPC 47A,
CC and a genetic mechanism for the deletion of the CH3 domain of the
CC mutant chain is proposed.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D11468; BAA02026.1; ALT_INIT; Genomic_DNA.
DR PIR; A91479; AHMS.
DR PDB; 7JG1; EM; 3.30 A; A/B/C/D=1-344.
DR PDB; 7JG2; EM; 3.30 A; A/B/C/D=1-344.
DR PDBsum; 7JG1; -.
DR PDBsum; 7JG2; -.
DR AlphaFoldDB; P01878; -.
DR SMR; P01878; -.
DR GlyGen; P01878; 4 sites.
DR iPTMnet; P01878; -.
DR CPTAC; non-CPTAC-3828; -.
DR jPOST; P01878; -.
DR MaxQB; P01878; -.
DR PeptideAtlas; P01878; -.
DR PRIDE; P01878; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01878; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IPI:AgBase.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR003599; Ig_sub.
DR Pfam; PF07654; C1-set; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Reference proteome; Repeat.
FT CHAIN <1..344
FT /note="Ig alpha chain C region"
FT /id="PRO_0000153568"
FT DOMAIN 6..99
FT /note="Ig-like 1"
FT DOMAIN 116..206
FT /note="Ig-like 2"
FT DOMAIN 219..321
FT /note="Ig-like 3"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941,
FT ECO:0000269|PubMed:6776528"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="O-linked (GalNAc) serine; in variant MOPC 47A"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; in variant M511"
FT /evidence="ECO:0000269|PubMed:6776528"
FT DISULFID 26..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 76..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 114..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 2
FT /note="S -> A (in MOPC 47A)"
FT VARIANT 18
FT /note="S -> C (in MOPC 47A and M511)"
FT VARIANT 67
FT /note="N -> S (in MOPC 47A and M511)"
FT VARIANT 73
FT /note="A -> T (in MOPC 47A)"
FT VARIANT 112
FT /note="P -> G (in M511; requires 2 nucleotide
FT substitutions)"
FT VARIANT 135
FT /note="S -> Q (in MOPC 47A and M511; requires 2 nucleotide
FT substitutions)"
FT VARIANT 141
FT /note="N -> D (in MOPC 47A and M511)"
FT VARIANT 168
FT /note="Q -> E (in MOPC 47A)"
FT VARIANT 212..213
FT /note="VT -> SQ (in MOPC 47A)"
FT VARIANT 235
FT /note="E -> G (in M511)"
FT VARIANT 255..290
FT /note="Missing (in M511)"
FT VARIANT 295
FT /note="T -> D (in M511; requires 2 nucleotide
FT substitutions)"
FT VARIANT 301
FT /note="Q -> G (in M511; requires 2 nucleotide
FT substitutions)"
FT VARIANT 329
FT /note="N -> Q (in M511; requires 2 nucleotide
FT substitutions)"
FT VARIANT 331
FT /note="S -> N (in M511)"
FT NON_TER 1
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 309..320
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 328..341
FT /evidence="ECO:0007829|PDB:7JG1"
SQ SEQUENCE 344 AA; 36876 MW; 3694CFFF9B19A9F8 CRC64;
ESARNPTIYP LTLPPALSSD PVIIGCLIHD YFPSGTMNVT WGKSGKDITT VNFPPALASG
GRYTMSNQLT LPAVECPEGE SVKCSVQHDS NPVQELDVNC SGPTPPPPIT IPSCQPSLSL
QRPALEDLLL GSDASITCTL NGLRNPEGAV FTWEPSTGKD AVQKKAVQNS CGCYSVSSVL
PGCAERWNSG ASFKCTVTHP ESGTLTGTIA KVTVNTFPPQ VHLLPPPSEE LALNELLSLT
CLVRAFNPKE VLVRWLHGNE ELSPESYLVF EPLKEPGEGA TTYLVTSVLR VSAETWKQGD
QYSCMVGHEA LPMNFTQKTI DRLSGKPTNV SVSVIMSEGD GICY
