ID Q9ESP3_RAT Unreviewed; 1851 AA. AC Q9ESP3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 02-SEP-2026, entry version 103. DE RecName: Full=Mucin-2 {ECO:0000256|ARBA:ARBA00067534}; DE Flags: Fragment; GN Name=Muc5ac {ECO:0000313|RGD:62001}; GN Synonyms=Muc5AC {ECO:0000313|EMBL:BAB17787.1}; 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 {ECO:0000313|EMBL:BAB17787.1}; RN [1] {ECO:0000313|EMBL:BAB17787.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar {ECO:0000313|EMBL:BAB17787.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAB17787.1}; RA Oinuma T., Suganuma T.; RT "Rat gastric mucin Muc5AC: Sequence of its 5'-region contains conserved D- RT domains and two leucine zipper motifs."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homomultimer; disulfide-linked. The N- and C-terminus mediate CC their assembly into higher order structures to form filaments. The CTCK CC domains of two polypeptides associate in the endoplasmic reticulum to CC generate intermolecularly disulfide-bonded dimers. These dimers CC progress to the Golgi apparatus, which is a more acidic environment CC than the endoplasmic reticulum. Under acidic conditions, the N-termini CC form non-covalent intermolecular interactions that juxtapose assemblies CC from different CTCK-linked dimers to produce long, disulfide-linked CC polymers that remain highly compact until secretion. CC {ECO:0000256|ARBA:ARBA00063950}. CC -!- SUBUNIT: Homomultimer; disulfide-linked. The N- and C-terminus mediate CC their assembly into higher order structures to form filaments. The CTCK CC domains of two polypeptides associate in the endoplasmic reticulum to CC generate intermolecularly disulfide-bonded dimers. These dimers CC progress to the Golgi apparatus, which is a more acidic environment CC than the endoplasmic reticulum. Under acidic conditions, the N-termini CC form non-covalent intermolecular interactions that juxtapose assemblies CC of the third VWD domain (VWD3) from different CTCK-linked dimers. The CC VWD3 assemblies then become disulfide bonded to one another to produce CC long, disulfide-linked polymers that remain highly compact until CC secretion. Interacts with FCGBP. Interacts with AGR2; disulfide-linked. CC {ECO:0000256|ARBA:ARBA00064609}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00580}. 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; AB042530; BAB17787.1; -; mRNA. DR MEROPS; I08.951; -. DR AGR; RGD:62001; -. DR RGD; 62001; Muc5ac. DR OrthoDB; 10071893at2759; -. DR PhylomeDB; Q9ESP3; -. DR GO; GO:0070701; C:mucus layer; IEA:UniProtKB-ARBA. DR CDD; cd19941; TIL; 3. DR FunFam; 2.10.25.10:FF:000153; MUC5B isoform 1; 1. DR FunFam; 2.10.25.10:FF:000674; Mucin-2; 1. DR FunFam; 2.10.25.10:FF:000414; von Willebrand factor; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR Gene3D; 2.10.25.10; Laminin; 3. DR InterPro; IPR050780; Mucin_vWF_Thrombospondin_sf. DR InterPro; IPR036084; Ser_inhib-like_sf. DR InterPro; IPR002919; TIL_dom. DR InterPro; IPR058753; TIL_OTOGL_Mucin. DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom. DR InterPro; IPR001007; VWF_dom. DR InterPro; IPR001846; VWF_type-D. DR InterPro; IPR025155; WxxW_domain. DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1. DR PANTHER; PTHR11339:SF401; MUCIN-5AC; 1. DR Pfam; PF08742; C8; 3. DR Pfam; PF13330; Mucin2_WxxW; 2. DR Pfam; PF01826; TIL; 2. DR Pfam; PF25962; TIL_OTOGL_Mucin; 1. DR Pfam; PF00094; VWD; 3. DR SMART; SM00832; C8; 3. DR SMART; SM00214; VWC; 3. DR SMART; SM00215; VWC_out; 2. DR SMART; SM00216; VWD; 3. DR SUPFAM; SSF57567; Serine protease inhibitors; 3. DR PROSITE; PS51233; VWFD; 3. PE 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00580}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..31 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 32..1851 FT /note="Mucin-2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004325089" FT DOMAIN 82..252 FT /note="VWFD" FT /evidence="ECO:0000259|PROSITE:PS51233" FT DOMAIN 435..610 FT /note="VWFD" FT /evidence="ECO:0000259|PROSITE:PS51233" FT DOMAIN 904..1075 FT /note="VWFD" FT /evidence="ECO:0000259|PROSITE:PS51233" FT REGION 1510..1590 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1753..1851 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1510..1533 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1534..1578 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1753..1772 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1773..1796 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1803..1851 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 459..609 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00580" FT DISULFID 481..489 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00580" FT NON_TER 1851 FT /evidence="ECO:0000313|EMBL:BAB17787.1" SQ SEQUENCE 1851 AA; 199405 MW; 879DE5B54929C52B CRC64; MLHSMGVGRR KLAPFWVLAL ALTFNQHTGQ ALEDTRKSHL EHYSDLSQPQ GHVGTPLNRV TIIPPLKTIP VVRAFNPAHT RRVCSTWGNF HYKTFDGQVF YFPGLCNYVF SEHCGAAYED FNIQLRRGLE SNSTTLSRVI MKLDGLVVEL TKSSVLVNNH PVQLPFSQSG VLIELSNGYL KVVARLGLVF MWNDDDSLLL ELDTKYANKT CGLCGDFNGS PESSEFLSHN VRLTPLEFGN FQKMDGPTEQ CQDPLPVPQK NCSIRSSICE EILKGQLFSN CAALVDISSY LEACQQDLCL CESSDPSNCI CHTLAEYSRQ CAHAGGQPQN WRGPNLCPQT CLLNMEYQEC GSPCVDTCSN PQHSQVCEDH CVAGCFCPEG MVLDDSNQTG CVPVSQCACL YNGTLYAPGT SYSTDCTKCT CSGGQWSCQE VPCSGTCSVM GGSHISTFDE RQYTVHGDCS YVLCKPYDSN AFTVLAELRK CGLTESETCL KTVTLNLGGG KTVITVKATG EVFVNQIYTQ LPVSTANATF FRPSTFFIIG QTNLGLQLEI QLHPIMQVSV RIAPEFRGLT SGLCGNFNSM QADDFQTISG VVEGTAAAFF NTFKTQAACP NVKNIFEDPC SLSVENEKYA QHWCSQLTDA NGPFSQCHAT VNPSTFFSNC MFDTCNCEKS EDCLCAALSS YVRACAAKGV LLSDWREGIC AKPTITCPKS MTYQYHISTC QPTCRSLSEE DVTCHVNFIP VDGCTCPKGT FLDDSGKCVQ ATSCPCYYKG SPVPNGESVH DNGAICTCTQ GALTCIGGPV LTPVCDAPMI YFDCRNATPG DTGAGCQKSC HTLDMTCYSS ECVPGCVCPN GLVADGNGSC VVAEDCPCVH NEATYRPGET IQVGCNNCTC ENRMWQCTDK PCLATCAVYG DGHYITFDGQ RYSFSGDCEY TLLQDNCGGN GSSQDAFRVV TENIPCGTTG TTCSKGIKIF LGSYELKLSD SKMEVVQKGV GQEPPYFVHQ MGNYLVVETD IGLVLLWDKK TSIFLRLSPE FKGKVCGLCG NFDDNAINDF TTRSQSVVSD MLEFGNSWKL SPSCPDASVS KDPCTANPYR KSWAQKQCSI INSAAFSACH AHVEPAKYYE ACVNDACACD SGGDCECFCT AVAAYAQACH EVGVCVSWRT PDICPLFCDY YNPEGQCEWH YQPCGAPCMR TCQNPTGQCL QDLRGLEGCY PKCPPTAPIF DEGTMQCVSN CTVSPSPCRV NGKLYRPGTP IPSDENCYSC VCTESGVNCT HDAGACVCTY NGQRYHPGDT IYHTTDGMGG CISAHCRDNG TIERIVDTCS STSPPPPTTF SFSTTLVMTS MQPSSTHSSP TPSVVYPGSP SKAVLTASSV SSVKTPETTS VLTTSTSAST LTMPACQEEC LWSPWMDISR PGRGIDSGDF DTLENLHAHG YQICPVPKAV ECRAEDNPGV PFHALQQHVE CSTTVGLICY NSDQVSGLCD NYQIKIQCCT PINCPTSTGP TQTTHLIVSR TSTMEDTTSS VPVTSTEHTY STVASSPSTH TPGPSPSSSV PSSSAPARST PTPVSSTTVK TTLPTTSPMP EPTSATSSVS ISTLGSTLAS PEITHGCRKE LCNWTDWIDG SYPEPGRSSG DFDTFVNLRA KGYKFCEKPW NVECRAQFFP NTPLQELGQD VTCSREVGLI CLNKNQLPPI CYNYEIRIEC CTIVNICSTT SATTQPTSHG VSIKTKTNWI TNTYSFSTEN TSGHSTVINT KTWVTGSTHT TPQPGTRPTP SIVSTQDTST SSVQTDSTTS SSHTSSPNTG RVSTTHTTHT SSPPTGGTSP TSTTHTSSPN TGGTSPTSTT HTSSPXTGGT S //