ID MUCB1_XENLA Reviewed; 398 AA. AC P38565; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 22-FEB-2023, entry version 83. DE RecName: Full=Integumentary mucin B.1; DE AltName: Full=FIM-B.1; DE Flags: Fragment; 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]. RX PubMed=2207068; DOI=10.1021/bi00478a018; RA Probst J.C., Gertzen E.-M., Hoffmann W.; RT "An integumentary mucin (FIM-B.1) from Xenopus laevis homologous with von RT Willebrand factor."; RL Biochemistry 29:6240-6244(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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02910; AAA49711.1; -; mRNA. DR PIR; A35281; A35281. DR AlphaFoldDB; P38565; -. DR Proteomes; UP000186698; Genome assembly. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR006208; Glyco_hormone_CN. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR47246; MUCIN-19; 1. DR PANTHER; PTHR47246:SF1; MUCIN-19; 1. DR Pfam; PF00007; Cys_knot; 1. DR SMART; SM00041; CT; 1. DR SMART; SM00214; VWC; 2. DR SUPFAM; SSF57603; FnI-like domain; 1. DR PROSITE; PS01185; CTCK_1; 1. DR PROSITE; PS01225; CTCK_2; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted. FT CHAIN <1..398 FT /note="Integumentary mucin B.1" FT /id="PRO_0000158961" FT REPEAT <1..7 FT /note="1" FT REPEAT 8..18 FT /note="2" FT REPEAT 19..29 FT /note="3" FT REPEAT 30..40 FT /note="4" FT REPEAT 41..51 FT /note="5" FT REPEAT 52..62 FT /note="6" FT REPEAT 66..76 FT /note="7" FT REPEAT 83..93 FT /note="8" FT DOMAIN 169..234 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 301..392 FT /note="CTCK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..93 FT /note="8 X 11 AA tandem repeats of G-E-S-T-P-A-P-S-E-T-T" FT COMPBIAS 1..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 301..356 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT DISULFID 323..370 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT DISULFID 332..386 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT DISULFID 336..388 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT DISULFID ?..391 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT NON_TER 1 SQ SEQUENCE 398 AA; 42101 MW; C06C86A805A3C3A4 CRC64; PAPSETTGES TPAPSETTGE STPAPSETTG ESTPAPSETT GESTPAPSET TGESTPAPSE TTVPSGESTP APSETTVPSV PSGESTPAPS ETTELRIIPP EVSTVAVPVT TGQITPAVTT EHSTEEILTL PPPVVGPVLP AKPTVDISKY TNTTTTKSTV PTTTIPPKAT CCGSSGESVQ AGHMWQTGCD VCTCNGTSGK TQCAPRQCEK EIICKSDERR VLRKPGKSCC GYCEPLTCKH NGTEYKLGAT FIDKSNPCIT YRCDASGLTV NVKSCPNEQV CSKSERTYDS DGCCFSCDTS CKPVPATVGI QGEYDYQNEK TNCSANIIMA KCSGQCQHKL TYDTIDNKVV TKCRCCKADR VEPRKAHLVC DNGKKKIYKY KHITSCKCTS CTAYNIRL //