MUA1_XENLA
ID MUA1_XENLA Reviewed; 400 AA.
AC P10667;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Integumentary mucin A.1;
DE AltName: Full=FIM-A.1;
DE AltName: Full=Preprospasmolysin;
DE Flags: Precursor;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=3372504; DOI=10.1016/s0021-9258(18)68553-9;
RA Hoffmann W.;
RT "A new repetitive protein from Xenopus laevis skin highly homologous to
RT pancreatic spasmolytic polypeptide.";
RL J. Biol. Chem. 263:7686-7690(1988).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2196180; DOI=10.1016/0014-4827(90)90230-8;
RA Hauser F., Gertzen E.M., Hoffmann W.;
RT "Expression of spasmolysin (FIM-A.1): an integumentary mucin from Xenopus
RT laevis.";
RL Exp. Cell Res. 189:157-162(1990).
CC -!- FUNCTION: Could be involved in defense against microbial infections.
CC Protects the epithelia from external environment.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed and stored exclusively in mature mucous
CC glands of the skin.
CC -!- PTM: Extensively O-glycosylated. Consist of about 70% carbohydrate and
CC 30% protein.
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DR EMBL; M19971; AAA49960.1; -; mRNA.
DR PIR; A28172; A28172.
DR RefSeq; NP_001081324.1; NM_001087855.1.
DR AlphaFoldDB; P10667; -.
DR SMR; P10667; -.
DR GeneID; 397775; -.
DR Xenbase; XB-GENE-22041701; FIM-A.1.L.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd00111; Trefoil; 4.
DR Gene3D; 4.10.110.10; -; 4.
DR InterPro; IPR017994; P_trefoil_chordata.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR PANTHER; PTHR13826; PTHR13826; 4.
DR Pfam; PF00088; Trefoil; 4.
DR PRINTS; PR00680; PTREFOIL.
DR SMART; SM00018; PD; 4.
DR SUPFAM; SSF57492; SSF57492; 4.
DR PROSITE; PS00025; P_TREFOIL_1; 3.
DR PROSITE; PS51448; P_TREFOIL_2; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..400
FT /note="Integumentary mucin A.1"
FT /id="PRO_0000023468"
FT DOMAIN 21..64
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 72..115
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REPEAT 127..135
FT /note="1-1"
FT REPEAT 136..144
FT /note="1-2"
FT REPEAT 145..153
FT /note="1-3"
FT REPEAT 154..162
FT /note="1-4"
FT REPEAT 163..171
FT /note="1-5"
FT REPEAT 172..180
FT /note="1-6"
FT REPEAT 181..189
FT /note="1-7"
FT REPEAT 190..198
FT /note="1-8"
FT REPEAT 199..207
FT /note="1-9"
FT REPEAT 208..216
FT /note="1-10"
FT REPEAT 217..225
FT /note="1-11"
FT REPEAT 226..234
FT /note="1-12"
FT REPEAT 235..243
FT /note="1-13"
FT REPEAT 244..252
FT /note="1-14"
FT REPEAT 253..261
FT /note="1-15; approximate"
FT REPEAT 272..275
FT /note="2-1"
FT REPEAT 276..279
FT /note="2-2"
FT REPEAT 280..283
FT /note="2-3"
FT REPEAT 284..287
FT /note="2-4"
FT REPEAT 288..291
FT /note="2-5"
FT REPEAT 292..295
FT /note="2-6"
FT REPEAT 296..299
FT /note="2-7"
FT DOMAIN 298..343
FT /note="P-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 351..394
FT /note="P-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 122..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..261
FT /note="15 X 9 AA approximate tandem repeats of [AV]-[SP]-T-
FT T-[AP]-E-T-T-T"
FT REGION 272..299
FT /note="7 X 4 AA repeats of E-T-T-T"
FT COMPBIAS 122..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 33..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 43..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 74..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 84..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 94..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 312..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 322..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 353..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 363..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 373..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 400 AA; 42641 MW; AC0A9F042713ECAB CRC64;
MKHIILCIHF LLMVVGLGQA QDCSVAPNMR VNCGYPTVTE ADCRAVGCCF DSSILNTKWC
FYNATAGPIK KLECSGDPTK RIDCGFPRIT EKQCILRGCC FDSSISGVKW CYARTVITTP
APDTTTASTT AETTTVPTTP ETTTVPTTPE TTTVPTTPET TTVPTTPETT TVPTTPETTT
VPTTPETTTV PTTPETTTVP TTPETTTVPT TPETTTVPTT PETTTVPTTP ETTTASTTAE
TTTVPTTPET TTEPTTTPTT DTTPPTLPPT PETTTETTTE TTTETTTETT TETTTETTTA
PPPECAADRV DCGYSGITQA DCEGKGCIFD STIPETKWCF YTEAEAPARK AECTVDPSVR
TDCGYPGITD KECREKGCCY DECIPDVIWC FEKAVPVVNS
