ID   HV384_HUMAN             Reviewed;         117 AA.
AC   P0DTW3;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Probable non-functional immunoglobulin heavy variable 1-38-4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=IGHV1-38-4 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.4,
GN   ECO:0000312|HGNC:HGNC:5560};
GN   Synonyms=IGHV1-C {ECO:0000303|PubMed:23541343};
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] (IMGT ALLELE IGHV1-38-4*01).
RX   PubMed=23541343; DOI=10.1016/j.ajhg.2013.03.004;
RA   Watson C.T., Steinberg K.M., Huddleston J., Warren R.L., Malig M.,
RA   Schein J., Willsey A.J., Joy J.B., Scott J.K., Graves T.A., Wilson R.K.,
RA   Holt R.A., Eichler E.E., Breden F.;
RT   "Complete haplotype sequence of the human immunoglobulin heavy-chain
RT   variable, diversity, and joining genes and characterization of allelic and
RT   copy-number variation.";
RL   Am. J. Hum. Genet. 92:530-546(2013).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9619395; DOI=10.1159/000019049;
RA   Lefranc M.P.;
RT   "IMGT (ImMunoGeneTics) locus on focus. A new section of Experimental and
RT   Clinical Immunogenetics.";
RL   Exp. Clin. Immunogenet. 15:1-7(1998).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=11340299; DOI=10.1159/000049189;
RA   Lefranc M.P.;
RT   "Nomenclature of the human immunoglobulin heavy (IGH) genes.";
RL   Exp. Clin. Immunogenet. 18:100-116(2001).
RN   [4]
RP   NOMENCLATURE.
RA   Lefranc M.P., Lefranc G.;
RT   "The Immunoglobulin FactsBook.";
RL   (In) Lefranc M.P., Lefranc G. (eds.);
RL   The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN   [5]
RP   REVIEW ON SOMATIC HYPERMUTATION.
RX   PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA   Teng G., Papavasiliou F.N.;
RT   "Immunoglobulin somatic hypermutation.";
RL   Annu. Rev. Genet. 41:107-120(2007).
RN   [6]
RP   REVIEW ON IMMUNOGLOBULINS.
RX   PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA   Schroeder H.W. Jr., Cavacini L.;
RT   "Structure and function of immunoglobulins.";
RL   J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN   [7]
RP   REVIEW ON FUNCTION.
RX   PubMed=22158414; DOI=10.1038/nri3128;
RA   McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT   "Molecular programming of B cell memory.";
RL   Nat. Rev. Immunol. 12:24-34(2012).
RN   [8]
RP   NOMENCLATURE.
RX   PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
RA   Lefranc M.P.;
RT   "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and Rise
RT   of Immunoinformatics.";
RL   Front. Immunol. 5:22-22(2014).
CC   -!- FUNCTION: Probable non-functional open reading frame (ORF) of V region
CC       of the variable domain of immunoglobulin heavy chains
CC       (PubMed:24600447). Non-functional ORF generally cannot participate in
CC       the synthesis of a productive immunoglobulin chain due to altered V-
CC       (D)-J or switch recombination and/or splicing site (at mRNA level)
CC       and/or conserved amino acid change (protein level) (PubMed:9619395).
CC       Immunoglobulins, also known as antibodies, are membrane-bound or
CC       secreted glycoproteins produced by B lymphocytes. In the recognition
CC       phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC       receptors which, upon binding of a specific antigen, trigger the clonal
CC       expansion and differentiation of B lymphocytes into immunoglobulins-
CC       secreting plasma cells. Secreted immunoglobulins mediate the effector
CC       phase of humoral immunity, which results in the elimination of bound
CC       antigens (PubMed:22158414, PubMed:20176268). The antigen binding site
CC       is formed by the variable domain of one heavy chain, together with that
CC       of its associated light chain. Thus, each immunoglobulin has two
CC       antigen binding sites with remarkable affinity for a particular
CC       antigen. The variable domains are assembled by a process called V-(D)-J
CC       rearrangement and can then be subjected to somatic hypermutations
CC       which, after exposure to antigen and selection, allow affinity
CC       maturation for a particular antigen (PubMed:20176268, PubMed:17576170).
CC       {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC       ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447,
CC       ECO:0000303|PubMed:9619395}.
CC   -!- SUBUNIT: Most probably, the immunoglobulin is not assembled due to
CC       incorrect folding of heavy chain (Probable). Immunoglobulins are
CC       composed of two identical heavy chains and two identical light chains;
CC       disulfide-linked. {ECO:0000303|PubMed:20176268, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC       ECO:0000303|PubMed:22158414}. Cell membrane
CC       {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC   -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC       IMGT allele IGHV1-38-4*01. {ECO:0000305}.
CC   -!- CAUTION: Most probably a non-functional protein that cannot participate
CC       to the synthesis of a productive immunoglobulin chain due to a mutation
CC       at position 115, corresponding to the second cysteine from the
CC       disulfide bridge, potentially leading to uncorrect folding
CC       (PubMed:9619395). Watson et al (PubMed:23541343) identified this gene
CC       on chromosome 14. However, it is not currently present on the reference
CC       genome assembly (GRCh38/hg38). {ECO:0000303|PubMed:9619395,
CC       ECO:0000305}.
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DR   EMBL; KF698736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DTW3; -.
DR   SMR; P0DTW3; -.
DR   GlyGen; P0DTW3; 1 site.
DR   GeneCards; IGHV1-38-4; -.
DR   HGNC; HGNC:5560; IGHV1-38-4.
DR   neXtProt; NX_P0DTW3; -.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin; Immunoglobulin domain; Membrane; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..117
FT                   /note="Probable non-functional immunoglobulin heavy
FT                   variable 1-38-4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000450572"
FT   DOMAIN          20..>117
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  13137 MW;  ED9B4BDFC31C76B0 CRC64;
     MDWNWRILFL VVATTGAHSQ VQLVQSWAEV RKSGASVKVS CSFSGFTITS YGIHWVQQSP
     GQGLEWMGWI NPGNGSPSYA KKFQGRFTMT RDMSTTTAYT DLSSLTSEDM AVYYYAR