SPAI_PIG
ID SPAI_PIG Reviewed; 187 AA.
AC P16225;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sodium/potassium ATPase inhibitor SPAI-2;
DE AltName: Full=Protein WAP-2;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 22-58, AND
RP PYROGLUTAMATE FORMATION AT GLN-22.
RC TISSUE=Duodenum;
RX PubMed=7673229; DOI=10.1074/jbc.270.38.22428;
RA Kuroki J., Hosoya T., Itakura M., Hirose S., Tamechika I., Yoshimoto T.,
RA Ghoneim M.A., Nara K., Kato A., Suzuki Y., Furukawa M., Tachibana S.;
RT "Cloning, characterization, and tissue distribution of porcine SPAI, a
RT protein with a transglutaminase substrate domain and the WAP motif.";
RL J. Biol. Chem. 270:22428-22433(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8636131; DOI=10.1074/jbc.271.12.7012;
RA Tamechika I., Itakura M., Saruta Y., Furukawa M., Kato A., Tachibana S.,
RA Hirose S.;
RT "Accelerated evolution in inhibitor domains of porcine elafin family
RT members.";
RL J. Biol. Chem. 271:7012-7018(1996).
RN [3]
RP PROTEIN SEQUENCE OF 127-187.
RC TISSUE=Duodenum;
RX PubMed=2553020; DOI=10.1016/0006-291x(89)91747-6;
RA Araki K., Kuroki J., Ito O., Kuwada M., Tachibana S.;
RT "Novel peptide inhibitor (SPAI) of Na+, K+-ATPase from porcine intestine.";
RL Biochem. Biophys. Res. Commun. 164:496-502(1989).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=2171523; DOI=10.1016/s0006-291x(05)80170-6;
RA Araki K., Kuwada M., Ito O., Kuroki J., Tachibana S.;
RT "Four disulfide bonds' allocation of Na+, K(+)-ATPase inhibitor (SPAI).";
RL Biochem. Biophys. Res. Commun. 172:42-46(1990).
CC -!- FUNCTION: Inhibits Na(+),K(+) ATPase by the competitive mode against
CC Na(+).
CC -!- TISSUE SPECIFICITY: Small intestine > large intestine. The plasma
CC contains the pro-SPAI form circulating.
CC -!- DOMAIN: The repetitive domain of pro-SPAI serves as a substrate for
CC transglutaminase.
CC -!- PTM: The short form (AA 127-187) may be an artifact due to the strongly
CC acidic conditions of the duodenum. The pro-SPAI form may be the native
CC form.
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DR EMBL; D17755; BAC21091.1; -; Genomic_DNA.
DR EMBL; D83667; BAA12037.1; -; mRNA.
DR EMBL; D50320; BAA08855.1; -; Genomic_DNA.
DR PIR; I46650; I46650.
DR RefSeq; NP_001004032.1; NM_001004032.2.
DR AlphaFoldDB; P16225; -.
DR SMR; P16225; -.
DR MEROPS; I17.002; -.
DR PeptideAtlas; P16225; -.
DR Ensembl; ENSSSCT00000045949; ENSSSCP00000048384; ENSSSCG00000033675.
DR Ensembl; ENSSSCT00070024435; ENSSSCP00070020221; ENSSSCG00070012487.
DR Ensembl; ENSSSCT00070024444; ENSSSCP00070020229; ENSSSCG00070012487.
DR GeneID; 445518; -.
DR KEGG; ssc:445518; -.
DR CTD; 445518; -.
DR GeneTree; ENSGT00530000064218; -.
DR OrthoDB; 1560605at2759; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Proteomes; UP000314985; Chromosome 17.
DR Bgee; ENSSSCG00000033675; Expressed in ileum and 14 other tissues.
DR ExpressionAtlas; P16225; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0007620; P:copulation; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR Gene3D; 4.10.75.10; -; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR002098; SVP_I.
DR InterPro; IPR019541; Trappin_transglut-bd_rpt.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF10511; Cementoin; 3.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR00003; 4DISULPHCORE.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR PROSITE; PS00313; SVP_I; 2.
DR PROSITE; PS51390; WAP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7673229"
FT PROPEP 22..126
FT /evidence="ECO:0000269|PubMed:2553020"
FT /id="PRO_0000041361"
FT CHAIN 127..187
FT /note="Sodium/potassium ATPase inhibitor SPAI-2"
FT /id="PRO_0000041362"
FT REPEAT 34..39
FT /note="1"
FT REPEAT 40..45
FT /note="2"
FT REPEAT 46..51
FT /note="3"
FT REPEAT 58..63
FT /note="4"
FT REPEAT 64..85
FT /note="SVP-1 clotting 1"
FT REPEAT 64..69
FT /note="5"
FT REPEAT 70..75
FT /note="6"
FT REPEAT 76..81
FT /note="7"
FT REPEAT 82..87
FT /note="8"
FT REPEAT 88..93
FT /note="9"
FT REPEAT 100..105
FT /note="10"
FT REPEAT 106..111
FT /note="11"
FT REPEAT 112..117
FT /note="12"
FT REPEAT 118..123
FT /note="13"
FT REPEAT 124..129
FT /note="14"
FT DOMAIN 139..187
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT REGION 28..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..129
FT /note="14 X 6 AA approximate tandem repeats"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7673229"
FT DISULFID 146..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:2171523"
FT DISULFID 153..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:2171523"
FT DISULFID 162..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:2171523"
FT DISULFID 168..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:2171523"
FT VARIANT 127..138
FT /note="Missing (in SPAI-1)"
FT VARIANT 148
FT /note="R -> G (in SPAI-3)"
FT VARIANT 156
FT /note="S -> G (in SPAI-3)"
SQ SEQUENCE 187 AA; 20471 MW; 12F5BD0813AF5E27 CRC64;
MRSRSFLVLV AVFLICETLV AQRLDRIRGP KGQGQDPVEG QDQDEGPGPV KVEILDIGQD
PVKGQDPVKG QDPVKGQDPV KGQDLVKSQD PVKAELPDIG QDVVKGHEPV EGQDPVNAQL
PDKVQDPVKA QPAVPGRFLL SKRGHCPRIL FRCPLSNPSN KCWRDYDCPG VKKCCEGFCG
KDCLYPK
