MUC2L_RAT
ID MUC2L_RAT Reviewed; 837 AA.
AC P98089;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Intestinal mucin-like protein;
DE Short=MLP;
DE Flags: Fragment;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RX PubMed=1371999; DOI=10.1016/s0021-9258(18)42780-9;
RA Xu G., Huan L.-J., Khatri I., Wang D., Bennick A., Fahim R.E.F.,
RA Forstner G.G., Forstner J.F.;
RT "cDNA for the carboxyl-terminal region of a rat intestinal mucin-like
RT peptide.";
RL J. Biol. Chem. 267:5401-5407(1992).
CC -!- SUBUNIT: Multimeric.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Coats the epithelia of the intestines.
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DR EMBL; M81920; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A42112; A42112.
DR AlphaFoldDB; P98089; -.
DR SMR; P98089; -.
DR STRING; 10116.ENSRNOP00000064975; -.
DR GlyGen; P98089; 14 sites.
DR PaxDb; P98089; -.
DR PRIDE; P98089; -.
DR RGD; 1594023; LOC682824.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P98089; -.
DR PhylomeDB; P98089; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00832; C8; 1.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 2.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57567; SSF57567; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted.
FT CHAIN <1..837
FT /note="Intestinal mucin-like protein"
FT /id="PRO_0000158959"
FT REPEAT 17..27
FT /note="1"
FT REPEAT 28..38
FT /note="2"
FT REPEAT 39..50
FT /note="3"
FT REPEAT 51..62
FT /note="4"
FT REPEAT 63..70
FT /note="5; truncated"
FT DOMAIN 141..324
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 472..543
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 581..648
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 732..817
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 17..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 17..70
FT /note="5 X 11 AA approximate tandem repeats"
FT REGION 149..837
FT /note="Probably important for disulfide-bond mediated mucin
FT polymerization (link domain)"
FT COMPBIAS 31..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 165..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 189..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 732..779
FT /evidence="ECO:0000250"
FT DISULFID 746..793
FT /evidence="ECO:0000250"
FT DISULFID 755..809
FT /evidence="ECO:0000250"
FT DISULFID 759..811
FT /evidence="ECO:0000250"
FT DISULFID ?..816
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 837 AA; 91500 MW; 6335BCDCAC897F35 CRC64;
VNCSVDCQLQ VFNWSCPSTP STPPPSTPTT PTSSQTTTPS TPSTTSSKST PSTPQSTSSK
STPSTPPKTT LPGCLDFDPP RQVNETWWLC NCTMAICKYD NVVEIVELEC NPPPMPTCSN
GLKPVRVPDP DGCCWHWECD CYCTGWGDPH FVTFDGLYYS YQGNCTYVLV EEITPTVDNF
GVYIDNYHCD ANDKVSCPRT LIVHHETQEV LIKTVHMMPI EVEVQVNKQL VALPYKKYGL
EVYQSGINFV VDIPRLGAQV SYNGLSFSIR LPYHLFGNNT KGQCGTCTNN TADDCILPSG
EIISNCEVAA DEWLVNDPSK PHCPHKGLTT KRPAITTPGP FPENCTVSPV CQLIMDSLFS
QCHPFVPPKH YYEACLFDSC FVAGSGMECA SVQAYAALCA QEGVCIDWRN HTQGACAVTC
PAHRQYQACG PSEEPTCQSS SPKNSTLLVE GCFCPEGTTK FAPGYDVCVK ICGCVGPDNV
PREFGEHFEF DCKDCVCLEG GSGIVCQPKK CARGNLTTCE EDGTYLVVEA DPDDKCCNTT
SCKCDPKRCK AERPSCLLGF EVKSEHVPGK CCPVYSCVPK GVCVHENAEY QPGSPVYSNK
CQDCVCTDSM DNSTQLNVIS CTHVPCNISC SSGFELVEVP GECCKKCQQT HCIIKRPEQQ
YIILKPGEIQ KNPNDRCTFF SCMKINNQLI SSVSNITCPD FDPSDCVPGS ITYMPNGCCK
TCIHNPNNTV PCSAIPVMKE ISYNGCAKNI SMNFCAGSCG TFAMYSAQAQ DLDHGCSCCR
EERTSVRMVS LDCPDGSKLS HSYTHIESCL CQGTVCELPQ AQQSRTRRSS PRLLGRK
