PIGR_EQUAS
ID PIGR_EQUAS Reviewed; 762 AA.
AC P0DUB1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Polymeric immunoglobulin receptor {ECO:0000303|PubMed:32251747};
DE Short=PIgR {ECO:0000303|PubMed:32251747};
DE Short=Poly-Ig receptor;
DE Contains:
DE RecName: Full=Secretory component {ECO:0000303|PubMed:32251747};
DE Flags: Precursor;
GN Name=PIGR;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=26373886; DOI=10.1038/srep14106;
RA Huang J., Zhao Y., Bai D., Shiraigol W., Li B., Yang L., Wu J., Bao W.,
RA Ren X., Jin B., Zhao Q., Li A., Bao S., Bao W., Xing Z., An A., Gao Y.,
RA Wei R., Bao Y., Bao T., Han H., Bai H., Bao Y., Zhang Y., Daidiikhuu D.,
RA Zhao W., Liu S., Ding J., Ye W., Ding F., Sun Z., Shi Y., Zhang Y.,
RA Meng H., Dugarjaviin M.;
RT "Donkey genome and insight into the imprinting of fast karyotype
RT evolution.";
RL Sci. Rep. 5:14106-14106(2015).
RN [2]
RP PROTEIN SEQUENCE OF 19-49; 110-163; 232-269; 279-290; 298-334; 386-405;
RP 471-489; 539-549; 556-565 AND 579-591, IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION AT ASN-83; ASN-135; ASN-291; ASN-423 AND ASN-530, AND
RP SUBCELLULAR LOCATION (SECRETORY COMPONENT).
RX PubMed=32251747; DOI=10.1016/j.ijbiomac.2020.03.253;
RA Gnanesh Kumar B.S., Rawal A.;
RT "Sequence characterization and N-glycoproteomics of secretory
RT immunoglobulin A from donkey milk.";
RL Int. J. Biol. Macromol. 155:605-613(2020).
RN [3]
RP PROTEIN SEQUENCE OF 20-39; 148-163; 232-269; 360-375; 459-489 AND 566-578,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION (SECRETORY
RP COMPONENT).
RX PubMed=21645650; DOI=10.1016/j.jprot.2011.05.036;
RA Cunsolo V., Muccilli V., Fasoli E., Saletti R., Righetti P.G., Foti S.;
RT "Poppea's bath liquor: the secret proteome of she-donkey's milk.";
RL J. Proteomics 74:2083-2099(2011).
CC -!- FUNCTION: [Polymeric immunoglobulin receptor]: Mediates selective
CC transcytosis of polymeric IgA and IgM across mucosal epithelial cells.
CC Binds polymeric IgA and IgM at the basolateral surface of epithelial
CC cells. The complex is then transported across the cell to be secreted
CC at the apical surface. During this process, a cleavage occurs that
CC separates the extracellular (known as the secretory component) from the
CC transmembrane segment. {ECO:0000250|UniProtKB:P01833}.
CC -!- FUNCTION: [Secretory component]: Through its N-linked glycans ensures
CC anchoring of secretory IgA (sIgA) molecules to mucus lining the
CC epithelial surface to neutralize extracellular pathogens. On its own
CC (free form) may act as a non-specific microbial scavenger to prevent
CC pathogen interaction with epithelial cells.
CC {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBUNIT: Interacts (mainly via CDR1-like domain) with dimeric IgA.
CC Interacts (mainly via CDR2-like domain) with pentameric IgM.
CC {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBUNIT: [Secretory component]: Either free or part of the secretory
CC IgA (sIgA) complex that consists of two, four or five IgA monomers, and
CC two additional non-Ig polypeptides, namely the JCHAIN and the secretory
CC component (the proteolytic product of PIGR). Free secretory component
CC interacts with bacterial antigens toxA of C. difficile and eae of E.
CC coli. {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell
CC membrane {ECO:0000250|UniProtKB:P01833}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secretory component]: Secreted
CC {ECO:0000269|PubMed:21645650, ECO:0000269|PubMed:32251747}.
CC -!- DOMAIN: The Ig-like V-type 1/D1 domain contains three complementarity
CC determining region-like loops CDR1-3, which mediate interaction with
CC IgA and IgM. {ECO:0000250|UniProtKB:P01833}.
CC -!- PTM: N-glycosylated. Carries predominantly biantennary complex type
CC glycans which are largely non-fucosylated. Sialylation with NeuAc is
CC common, except for Asn-291 which carries exclusively high mannose
CC glycans. N-glycans attached to Asn-83: Gal2GlcNAc2Man3GlcNAc2;
CC Gal2GlcNAc2Man3GlcNAc2(Fuc); Gal1GlcNAc1Man4GlcNAc2(Fuc);
CC Gal1GlcNAc1Man3GlcNAc2; Gal1GlcNAc1Man4GlcNAc2 and
CC NeuAc1Gal2GlcNAc2Man3GlcNAc2. N-glycans attached to Asn-135:
CC Gal2GlcNAc2Man3GlcNAc2; Gal1GlcNAc1Man3GlcNAc2 and
CC NeuAc1Gal2GlcNAc2Man3GlcNAc2. N-glycans attached to Asn-291: Man5-
CC 8GlcNAc2. N-glycans attached to Asn-423: NeuAc1Gal2GlcNAc2Man3GlcNAc2.
CC N-glycans attached to Asn-530: Gal2GlcNAc2Man3GlcNAc2;
CC Gal1GlcNAc1Man3GlcNAc2 and NeuAc1Gal2GlcNAc2Man3GlcNAc2. N-
CC glycosylation is required for anchoring IgA molecules to mucus but is
CC not necessary for Ig binding. {ECO:0000269|PubMed:32251747}.
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DR RefSeq; XP_014684365.1; XM_014828879.1.
DR RefSeq; XP_014684370.1; XM_014828884.1.
DR RefSeq; XP_014684378.1; XM_014828892.1.
DR AlphaFoldDB; P0DUB1; -.
DR SMR; P0DUB1; -.
DR GeneID; 106823294; -.
DR KEGG; eai:106823294; -.
DR CTD; 5284; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 5.
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; 5.
DR SMART; SM00409; IG; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..762
FT /note="Polymeric immunoglobulin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451035"
FT CHAIN 19..602
FT /note="Secretory component"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT /id="PRO_0000451036"
FT TOPO_DOM 19..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..120
FT /note="Ig-like V-type 1; required for binding to polymeric
FT IgA and IgM"
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 145..238
FT /note="Ig-like V-type 2"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 251..351
FT /note="Ig-like V-type 3"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 363..460
FT /note="Ig-like V-type 4"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 464..563
FT /note="Ig-like V-type 5"
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 604..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT DISULFID 40..110
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 56..64
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..221
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 258..324
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..280
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 370..443
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 384..394
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 484..546
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 488..522
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 498..505
FT /evidence="ECO:0000250|UniProtKB:P01833,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 505
FT /note="Interchain (with C-184 IGHA/constant region of IgA
FT heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01833"
SQ SEQUENCE 762 AA; 82964 MW; 051387644A760607 CRC64;
MTLFFLTCLL AVFPVVSMKS PIFGPPEIDS VEGTSTSIKC YYPPTSVNRH SRKYWCRQGP
KGQCITLISS NGYVSKDYEG RANLTNFPES GTFVVNVDHL IQGDSGSYKC GVGINNRGLS
FDVRLRVVPG SGVLNGTQVY AEDLGGKVSI SCPFTSANLP NVKSVCKQIA DKHCVRVIDS
AGYKEPSYEG RAKLIIQGTT QTEFFFIIDQ LQVEDDGKYV CQAGDDSSGD KSNVDLHVLK
PEPELVYADL GSSVRFDCAL GPEVVNVAKF LCQKNKEKTC NLVANTLGQR NQTFKGRILS
QNNNGVFSVD ITNLRKEDAG LYLCGANSDG QPQKSRPIQA WQLFVNEETT FPSRPSVVKG
VVGGSVAVLC PYNPKEVNSV KSWCRWEDTQ NGGCPLLVQS TGLVKNQYEQ YNGRLVLYDE
PGNGTYTVIL NQLTAQDAGF YWCLTNGDIH WRSTVELKIV EGQPNLKVPK TVNVELGETV
QLTCHSPCKF YSYKKFWCKW TDQGCSALPS QDEGSGQAVV NCDQNSQLIN LTLKQVTKGD
EGWYWCGVKE GLQYKETVAV YVAVKEKGTG SGALSSVRAA PAEDVIETSV RKVDRKVVQD
PRLFVDTQAK DPEDAAGGSI ASADPGSSAG QGGSSKVVVS TLVPLALVLA LGVLVVGVLR
ARHRKNVDRI SIRSYRTDIS MSDFENSRDF GANDNMGASP VSQETTLGGK DEFIATTENT
VETEEPKKAK RSSKEEADMA YTAFLLQANN MAANIQDGPS KA
