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P98088

- MUC5A_HUMAN

UniProt

P98088 - MUC5A_HUMAN

Protein

Mucin-5AC

Gene

MUC5AC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    Gel-forming glycoprotein of gastric and respiratoy tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microrganisms and particles that are subsequently removed by the mucocilary system.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei4302 – 43032Cleavage

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. extracellular fibril organization Source: MGI
    3. O-glycan processing Source: Reactome
    4. post-translational protein modification Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    REACT_115835. Termination of O-glycan biosynthesis.

    Protein family/group databases

    MEROPSiI08.951.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mucin-5AC
    Short name:
    MUC-5AC
    Alternative name(s):
    Gastric mucin
    Lewis B blood group antigen
    Short name:
    LeB
    Major airway glycoprotein
    Mucin-5 subtype AC, tracheobronchial
    Tracheobronchial mucin
    Short name:
    TBM
    Gene namesi
    Name:MUC5AC
    Synonyms:MUC5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:7515. MUC5AC.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. fibril Source: MGI
    3. Golgi lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2122 – 21221W → A: No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum. 1 Publication
    Mutagenesisi4302 – 43021D → A or E: Abolishes cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 50305003Mucin-5ACPRO_0000158957Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi? ↔ 4995By similarity
    Disulfide bondi103 ↔ 111By similarity
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi456 ↔ 464By similarity
    Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1308 – 13081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1389 – 13891C-linked (Man)Curated
    Glycosylationi1584 – 15841C-linked (Man)Curated
    Glycosylationi1749 – 17491C-linked (Man)Curated
    Glycosylationi1957 – 19571C-linked (Man)Curated
    Glycosylationi2122 – 21221C-linked (Man)
    Glycosylationi2652 – 26521C-linked (Man)Curated
    Glycosylationi2950 – 29501C-linked (Man)Curated
    Glycosylationi3198 – 31981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3383 – 33831C-linked (Man)Curated
    Glycosylationi4009 – 40091C-linked (Man)Curated
    Glycosylationi4245 – 42451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4318 – 43181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4433 – 44331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4469 – 44691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4612 – 46121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4723 – 47231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4753 – 47531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4762 – 47621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4831 – 48311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4904 – 49041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4908 ↔ 4958By similarity
    Disulfide bondi4922 ↔ 4972By similarity
    Disulfide bondi4933 ↔ 4988By similarity
    Disulfide bondi4937 ↔ 4990By similarity
    Glycosylationi4967 – 49671N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    C-, O- and N-glycosylated. O-glycosylated on the Thr-/Ser-rich tandem repeats. C-mannosylation in the Cys-rich subdomains may be required for proper folding of these regions and for export from the endoplasmic reticulum during biosynthesis.1 Publication
    Proteolytic cleavage in the C-terminal is initiated early in the secretory pathway and does not involve a serine protease. The extent of cleavage is increased in the acidic parts of the secretory pathway. Cleavage generates a reactive group which could link the protein to a primary amide.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP98088.
    PRIDEiP98088.

    PTM databases

    UniCarbKBiP98088.

    Expressioni

    Tissue specificityi

    Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum.2 Publications

    Gene expression databases

    GenevestigatoriP98088.

    Organism-specific databases

    HPAiCAB002774.
    CAB009395.
    HPA040615.

    Interactioni

    Subunit structurei

    Multimeric. Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD).1 Publication

    Protein-protein interaction databases

    IntActiP98088. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP98088.
    SMRiP98088. Positions 336-394, 800-873, 4589-4652, 4903-4994.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 281202VWFD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 647215VWFD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini902 – 1109208VWFD 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati1383 – 148199Cys-rich subdomain 1Add
    BLAST
    Repeati1577 – 1677101Cys-rich subdomain 2Add
    BLAST
    Repeati1743 – 1847105Cys-rich subdomain 3Add
    BLAST
    Repeati1950 – 2050101Cys-rich subdomain 4Add
    BLAST
    Repeati2116 – 2220105Cys-rich subdomain 5Add
    BLAST
    Repeati2646 – 2750105Cys-rich subdomain 6Add
    BLAST
    Repeati2944 – 3084141Cys-rich subdomain 7Add
    BLAST
    Repeati3377 – 3481105Cys-rich subdomain 8Add
    BLAST
    Repeati4003 – 4107105Cys-rich subdomain 9Add
    BLAST
    Domaini4296 – 4507212VWFD 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini4652 – 472170VWFC 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini4757 – 482468VWFC 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini4908 – 499689CTCKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1383 – 410727259 X Cys-rich subdomain repeatsAdd
    BLAST
    Regioni2257 – 262436846 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
    BLAST
    Regioni2787 – 292213617 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
    BLAST
    Regioni3085 – 335527134 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
    BLAST
    Regioni3517 – 397145558 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1193 – 11953Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4896 – 49016Poly-Pro

    Domaini

    The cysteine residues in the Cys-rich subdomain repeats are not involved in disulfide bonding.

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 2 VWFC domains.PROSITE-ProRule annotation
    Contains 4 VWFD domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    InParanoidiP98088.

    Family and domain databases

    InterProiIPR006207. Cys_knot_C.
    IPR002919. TIL_dom.
    IPR014853. Unchr_dom_Cys-rich.
    IPR001007. VWF_C.
    IPR001846. VWF_type-D.
    IPR025155. WxxW_domain.
    [Graphical view]
    PfamiPF08742. C8. 4 hits.
    PF13330. Mucin2_WxxW. 9 hits.
    PF01826. TIL. 3 hits.
    PF00094. VWD. 4 hits.
    [Graphical view]
    SMARTiSM00832. C8. 4 hits.
    SM00041. CT. 1 hit.
    SM00214. VWC. 6 hits.
    SM00216. VWD. 4 hits.
    [Graphical view]
    SUPFAMiSSF57567. SSF57567. 4 hits.
    PROSITEiPS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS01208. VWFC_1. 2 hits.
    PS50184. VWFC_2. 2 hits.
    PS51233. VWFD. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragments.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P98088-1 [UniParc]FASTAAdd to Basket

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    MSVGRRKLAL LWALALALAC TRHTGHAQDG SSESSYKHHP ALSPIARGPS     50
    GVPLRGATVF PSLRTIPVVR ASNPAHNGRV CSTWGSFHYK TFDGDVFRFP 100
    GLCNYVFSEH CGAAYEDFNI QLRRSQESAA PTLSRVLMKV DGVVIQLTKG 150
    SVLVNGHPVL LPFSQSGVLI QQSSSYTKVE ARLGLVLMWN HDDSLLLELD 200
    TKYANKTCGL CGDFNGMPVV SELLSHNTKL TPMEFGNLQK MDDPTEQCQD 250
    PVPEPPRNCS TGFGICEELL HGQLFSGCVA LVDVGSYLEA CRQDLCFCED 300
    TDLLSCVCHT LAEYSRQCTH AGGLPQDWRG PDFCPQKCPN NMQYHECRSP 350
    CADTCSNQEH SRACEDHCVA GCFCPEGTVL DDIGQTGCVP VSKCACVYNG 400
    AAYAPGATYS TDCTNCTCSG GRWSCQEVPC PDTCSVLGGA HFSTFDGKQY 450
    TVHGDCSYVL TKPCDSSAFT VLAELRRCGL TDSETCLKSV TLSLDGAQTV 500
    VVIKASGEVF LNQIYTQLPI SAANVTIFRP STFFIIAQTS LGLQLNLQPV 550
    PTMQLFMQLA PKLRGQTCGL CGNFNSIQAD DFRTLSGVVE ATAAAFFNTF 600
    KTQAACPNIR NSFEDPCSLS VENEKYAQHW CSQLTDADGP FGRCHAAVKP 650
    GTYYSNCVFD TCNCERSEDC LCAALSSYVH ACAAKGVQLG GWRDGVCTKP 700
    MTTCPKSMTY HYHVSTCQPT CRSLSEGDIT CSVGFIPVDG CICPKGTFLD 750
    DTGKCVQASN CPCYHRGSMI PNGESVHDSG AICTCTHGKL SCIGGQAPAP 800
    VCAAPMVFFD CRNATPGDTG AGCQKSCHTL DMTCYSPQCV PGCVCPDGLV 850
    ADGEGGCITA EDCPCVHNEA SYRAGQTIRV GCNTCTCDSR MWRCTDDPCL 900
    ATCAVYGDGH YLTFDGQSYS FNGDCEYTLV QNHCGGKDST QDSFRVVTEN 950
    VPCGTTGTTC SKAIKIFLGG FELKLSHGKV EVIGTDESQE VPYTIQQMGI 1000
    YLVVDTDIGL VLLWDKKTSI FINLSPEFKG RVCGLCGNFD DIAVNDFATR 1050
    SRSVVGDVLE FGNSWKLSPS CPDALAPKDP CTANPFRKSW AQKQCSILHG 1100
    PTFAACHAHV EPARYYEACV NDACACDSGG DCECFCTAVA AYAQACHEVG 1150
    LCVCLRTPSI CPLFCDYYNP EGQCEWHYQP CGVPCLRTCR NPRGDCLRDV 1200
    RGLEGCYPKC PPEAPIFDED KMQCVATCPT PPLPPRCHVH GKSYRPGAVV 1250
    PSDKNCQSCL CTERGVECTY KAEACVCTYN GQRFHPGDVI YHTTDGTGGC 1300
    ISARCGANGT IERRVYPCSP TTPVPPTTFS FSTPPLVVSS THTPSNGPSS 1350
    AHTGPPSSAW PTTAGTSPRT RLPTASASLP PVCGEKCLWS PWMDVSRPGR 1400
    GTDSGDFDTL ENLRAHGYRV CESPRSVECR AEDAPGVPLR ALGQRVQCSP 1450
    DVGLTCRNRE QASGLCYNYQ IRVQCCTPLP CSTSSSPAQT TPPTTSKTTE 1500
    TRASGSSAPS STPGTVSLST ARTTPAPGTA TSVKKTFSTP SPPPVPATST 1550
    SSMSTTAPGT SVVSSKPTPT EPSTSSCLQE LCTWTEWIDG SYPAPGINGG 1600
    DFDTFQNLRD EGYTFCESPR SVQCRAESFP NTPLADLGQD VICSHTEGLI 1650
    CLNKNQLPPI CYNYEIRIQC CETVNVCRDI TRLPKTVATT RPTPHPTGAQ 1700
    TQTTFTTHMP SASTEQPTAT SRGGPTATSV TQGTHTTLVT RNCHPRCTWT 1750
    KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRV QCRAKSHPEV 1800
    SIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPRGCHMT 1850
    STPGSTSSSP AQTTPSTTSK TTEIQASGSS APSSTPGTVS LSTARTTPAP 1900
    GTATSVKKTF STPSPPPVPA TSTSSMSTTA PGTSVVSSKP TPTEPSTSSC 1950
    LQELCTWTEW IDGSYPAPGI NGGDFDTFQN LRDEGYTFCE SPRSVQCRAE 2000
    SFPNTPLGRL GQDVICSHTE GLICLNKNQL PPICYNYEIR IQCCETVNVC 2050
    RDITRPPKTV ATTRPTPHPT GAQTQTTFTT HMPSASTEQP TATSRGGPTA 2100
    TSVTQGTHTT PVTRNCHPRC TWTTWFDVDF PSPGPHGGDK ETYNNIIRSG 2150
    EKICRRPEEI TRLQCRAKSH PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP 2200
    FKMCLNIEVR VLCCETPKGC PVTSTPVTAP STPSGRAISP TQSTSSWQKS 2250
    RTTTLVTTST TSTPQTSTTY AHTTSTTSAP TARTTSAPTT STTSVPTTST 2300
    ISGPKTTPSP VPTTSTTSAA TTSTISAPTT STTSVPGTTP SPVLTTSTTS 2350
    APTTRTTSAS PAGTTSGPGN TPSPVPTTST ISAPTTSITS APTTSTTSAP 2400
    TSSTTSGPGT TPSPVPTTSI TSAPTTSTTS APTTSTTSAP TTSTTSAPTT 2450
    STTSAPTTST TSTPTSSTTS TPQTSTTSAS TTSITSGPGT TPSPVPTTST 2500
    TSAPTTSTTS AATTSTISAP TTSTTSAPTT STTSASTASK TSGLGTTPSP 2550
    IPTTSTTSPP TTSTTSASTA SKTSGPGTTP SPVPTTSTIF APRTSTTSAS 2600
    TTSTTPGPGT TPSPVPTTST ASVSKTSTSH VSISKTTHSQ PVTRDCHLRC 2650
    TWTKWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI TRLQCRAESH 2700
    PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNYEVR VLCCETPKGC 2750
    PVTSTPVTAP STPSGRATSP TQSTSSWQKS RTTTLVTTST TSTPQTSTTS 2800
    APTTSTTSAP TTSTTSAPTT STTSTPQTSI SSAPTSSTTS APTSSTISAR 2850
    TTSIISAPTT STTSSPTTST TSATTTSTTS APTSSTTSTP QTSKTSAATS 2900
    STTSSSGTTP SPVTTTSTAS VSKTSTSHVS VSKTTHSQPV TRDCHPRCTW 2950
    TKWFDVDFPS PGPHGGDKET YNNIIRSGEK ICRRPQEITR LQCRAKSHPE 3000
    VSIEHLGQVV QCSREEGLVC RNQDQQGPFK MCLNYEVRVL CCETPKGCPV 3050
    TSTSVTAPSP LVGEPPAQTQ STSSWQKSRT TTLVTSSITS TTQTSTTSAP 3100
    TTSTTPASIP STTSAPTTST TSAPTTSTTS APTTSTTSTP QTTTSSAPTS 3150
    STTSAPTTST ISAPTTSTIS APTTSTTSAP TASTTSAPTS TSSAPTTNTT 3200
    SAPTTSTTSA PITSTISAPT TSTTSTPQTS TISSPTTSTT PTPQTSTTSS 3250
    PTTSTTSAPT TSTTSAPTTS TTSTPQTSIS SAPTSSTTSA PTASTISAPT 3300
    TSTTSFHTTS TTSPPTSSTS STPQTSKTSA ATSSTTSGSG TTPSPVPTTS 3350
    TASVSKTSTS HVSVSKTTHS QPVTRDCHPR CTWTKWFDVD FPSPGPHGGD 3400
    KETYNNIIRS GEKICRRPEE ITRLQCRAES HPEVSIEHLG QVVQCSREEG 3450
    LVCRNQDQQG PFKMCLNYEV RVLCCETPKG CPVTSTPVTA PSTPSGRATS 3500
    PTQSTSSWQK SRTTTLVTTS TTSTPQTSTT SAPTTSTIPA STPSTTSAPT 3550
    TSTTSAPTTS TTSAPTHRTT SGPTTSTTLA PTTSTTSAPT TSTNSAPTTS 3600
    TISASTTSTI SAPTTSTISS PTSSTTSTPQ TSKTSAATSS TTSGSGTTPS 3650
    PVPTTSTTSA STTSTTSAPT TSTTSGPGTT PSPVPSTSIT SAATTSTTSA 3700
    PTTRTTSAPT SSMTSGPGTT PSPVPTTSTT SAPTTSTTSG PGTTPSPVPT 3750
    TSTTSAPITS TTSGPGSTPS PVPTTSTTSA PTTSTTSAST ASTTSGPTTS 3800
    TTSASTTSTI SPLTTSTTSA PITSMPSGPG TTPSPVPTTS TTSAPTTSTT 3850
    SGPGTTPSPV PTTSTTSAPT TSTTSASTAS TTSGPGTTPS PVPTTSTTSA 3900
    PTTSTTSAST ASTTSGPGTS LSPVPTTSTT SAPTTSTTSG PGTTPSPVPT 3950
    TSTTSAPTTS TTSGPGTTPS PVPTTSTTPV SKTSTSHLSV SKTTHSQPVT 4000
    SDCHPLCAWT KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRL 4050
    QCRAESHPEV NIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC 4100
    CETPRGCPVT SVTPYGTSPT NALYPSLSTS MVSASVASTS VASSSVASSS 4150
    VAYSTQTCFC NVADRLYPAG STIYRHRDLA GHCYYALCSQ DCQVVRGVDS 4200
    DCPSTTLPPA PATSPSISTS EPVTELGCPN AVPPRKKGET WATPNCSEAT 4250
    CEGNNVISLS PRTCPRVEKP TCANGYPAVK VADQDGCCHH YQCQCVCSGW 4300
    GDPHYITFDG TYYTFLDNCT YVLVQQIVPV YGHFRVLVDN YFCGAEDGLS 4350
    CPRSIILEYH QDRVVLTRKP VHGVMTNEII FNNKVVSPGF RKNGIVVSRI 4400
    GVKMYATIPE LGVQVMFSGL IFSVEVPFSK FANNTEGQCG TCTNDRKDEC 4450
    RTPRGTVVAS CSEMSGLWNV SIPDQPACHR PHPTPTTVGP TTVGSTTVGP 4500
    TTVGSTTVGP TTPPAPCLPS PICHLILSKV FEPCHTVIPP LLFYEGCVFD 4550
    RCHMTDLDVV CSSLELYAAL CASHDICIDW RGRTGHMCPF TCPADKVYQP 4600
    CGPSNPSYCY GNDSASLGAL REAGPITEGC FCPEGMTLFS TSAQVCVPTG 4650
    CPRCLGPHGE PVKVGHTVGM DCQECTCEAA TWTLTCRPKL CPLPPACPLP 4700
    GFVPVPAAPQ AGQCCPQYSC ACNTSRCPAP VGCPEGARAI PTYQEGACCP 4750
    VQNCSWTVCS INGTLYQPGA VVSSSLCETC RCELPGGPPS DAFVVSCETQ 4800
    ICNTHCPVGF EYQEQSGQCC GTCVQVACVT NTSKSPAHLF YPGETWSDAG 4850
    NHCVTHQCEK HQDGLVVVTT KKACPPLSCS LDEARMSKDG CCRFCPLPPP 4900
    PYQNQSTCAV YHRSLIIQQQ GCSSSEPVRL AYCRGNCGDS SSMYSLEGNT 4950
    VEHRCQCCQE LRTSLRNVTL HCTDGSSRAF SYTEVEECGC MGRRCPAPGD 5000
    TQHSEEAEPE PSQEAESGSW ERGVPVSPMH 5030
    Length:5,030
    Mass (Da):526,608
    Last modified:October 23, 2007 - v3
    Checksum:i00523008FF20ACAB
    GO

    Sequence cautioni

    The sequence AAA18431.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAC15950.1 differs from that shown. Reason: Frameshift at positions 24, 44, 671 and 683.
    The sequence CAA88307.1 differs from that shown. Reason: Frameshift at position 5024.
    The sequence CAH56330.1 differs from that shown. Reason: Frameshift at position 4616.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211S → R in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti432 – 4321D → G in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti549 – 5491P → L in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti658 – 6581V → M in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti702 – 7021T → I in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti716 – 7161T → A in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti817 – 8182GD → RG in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti869 – 8691E → K in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti978 – 9781G → R in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti996 – 9961Q → R in AAC15950. (PubMed:9506983)Curated
    Sequence conflicti1803 – 18031E → N AA sequence (PubMed:2656675)Curated
    Sequence conflicti2176 – 21761E → N AA sequence (PubMed:2656675)Curated
    Non-adjacent residuesi2448 – 24492Curated
    Sequence conflicti3004 – 30041E → N AA sequence (PubMed:2656675)Curated
    Non-adjacent residuesi3797 – 37982Curated
    Sequence conflicti3990 – 39912VS → HE in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4203 – 42031P → R in CAA88307. (PubMed:7775418)Curated
    Sequence conflicti4260 – 42623SPR → RPP in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4275 – 42751G → A in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4389 – 43891G → A in CAA88307. (PubMed:7775418)Curated
    Sequence conflicti4457 – 44604VVAS → HASA in AAH33831. (PubMed:15489334)Curated
    Sequence conflicti4524 – 45241H → Q in CAA04737. (PubMed:9620876)Curated
    Sequence conflicti4524 – 45241H → Q in CAA04738. (PubMed:9620876)Curated
    Sequence conflicti4569 – 45691A → R in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4621 – 46211R → P in CAA88307. (PubMed:7775418)Curated
    Sequence conflicti4640 – 46401S → T in CAA04737. (PubMed:9620876)Curated
    Sequence conflicti4640 – 46401S → T in CAA04738. (PubMed:9620876)Curated
    Sequence conflicti4732 – 47321G → R in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4739 – 47391A → R in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4809 – 48091G → R in AAA18431. (PubMed:7513696)Curated
    Sequence conflicti4922 – 49221C → S in AAA18431. (PubMed:7513696)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4897 – 48971L → P.2 Publications
    Corresponds to variant rs1132436 [ dbSNP | Ensembl ].
    VAR_036832

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ298317 mRNA. Translation: CAC83674.1.
    AJ298318 Genomic DNA. Translation: CAC83675.1.
    AJ298319 Genomic DNA. Translation: CAC83676.1.
    AF015521 mRNA. Translation: AAC15950.1. Frameshift.
    X81649 mRNA. Translation: CAA57309.1.
    AJ001402 mRNA. Translation: CAA04737.1.
    AJ001403 Genomic DNA. Translation: CAA04738.1.
    U06711 mRNA. Translation: AAA18431.1. Frameshift.
    Z48314 mRNA. Translation: CAA88307.1. Frameshift.
    BC033831 mRNA. Translation: AAH33831.1.
    AL833060 mRNA. Translation: CAH56330.1. Frameshift.
    PIRiA33811.
    JE0095.
    UniGeneiHs.534332.
    Hs.558950.
    Hs.721515.

    Polymorphism databases

    DMDMi160370004.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Mucin database
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ298317 mRNA. Translation: CAC83674.1 .
    AJ298318 Genomic DNA. Translation: CAC83675.1 .
    AJ298319 Genomic DNA. Translation: CAC83676.1 .
    AF015521 mRNA. Translation: AAC15950.1 . Frameshift.
    X81649 mRNA. Translation: CAA57309.1 .
    AJ001402 mRNA. Translation: CAA04737.1 .
    AJ001403 Genomic DNA. Translation: CAA04738.1 .
    U06711 mRNA. Translation: AAA18431.1 . Frameshift.
    Z48314 mRNA. Translation: CAA88307.1 . Frameshift.
    BC033831 mRNA. Translation: AAH33831.1 .
    AL833060 mRNA. Translation: CAH56330.1 . Frameshift.
    PIRi A33811.
    JE0095.
    UniGenei Hs.534332.
    Hs.558950.
    Hs.721515.

    3D structure databases

    ProteinModelPortali P98088.
    SMRi P98088. Positions 336-394, 800-873, 4589-4652, 4903-4994.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P98088. 1 interaction.

    Protein family/group databases

    MEROPSi I08.951.

    PTM databases

    UniCarbKBi P98088.

    Polymorphism databases

    DMDMi 160370004.

    Proteomic databases

    MaxQBi P98088.
    PRIDEi P98088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC11P001151.
    H-InvDB HIX0201650.
    HGNCi HGNC:7515. MUC5AC.
    HPAi CAB002774.
    CAB009395.
    HPA040615.
    MIMi 158373. gene.
    neXtProti NX_P98088.
    GenAtlasi Search...

    Phylogenomic databases

    InParanoidi P98088.

    Enzyme and pathway databases

    Reactomei REACT_115606. O-linked glycosylation of mucins.
    REACT_115835. Termination of O-glycan biosynthesis.

    Miscellaneous databases

    NextBioi 125477.
    PROi P98088.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P98088.

    Family and domain databases

    InterProi IPR006207. Cys_knot_C.
    IPR002919. TIL_dom.
    IPR014853. Unchr_dom_Cys-rich.
    IPR001007. VWF_C.
    IPR001846. VWF_type-D.
    IPR025155. WxxW_domain.
    [Graphical view ]
    Pfami PF08742. C8. 4 hits.
    PF13330. Mucin2_WxxW. 9 hits.
    PF01826. TIL. 3 hits.
    PF00094. VWD. 4 hits.
    [Graphical view ]
    SMARTi SM00832. C8. 4 hits.
    SM00041. CT. 1 hit.
    SM00214. VWC. 6 hits.
    SM00216. VWD. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57567. SSF57567. 4 hits.
    PROSITEi PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS01208. VWFC_1. 2 hits.
    PS50184. VWFC_2. 2 hits.
    PS51233. VWFD. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human mucin gene MUC5AC: organization of its 5'-region and central repetitive region."
      Escande F., Aubert J.-P., Porchet N., Buisine M.P.
      Biochem. J. 358:763-772(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2448, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2449-3797, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3798-4169.
    2. "Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC mucin gene and transcriptional up-regulation by bacterial exoproducts."
      Li D., Gallup M., Fan N., Szymkowski D.E., Basbaum C.B.
      J. Biol. Chem. 273:6812-6820(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1104.
      Tissue: Trachea.
    3. "Cloning and analysis of human gastric mucin cDNA reveals two types of conserved cysteine-rich domains."
      Klomp L.W., Van Rens L., Strous G.J.
      Biochem. J. 308:831-838(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1854.
    4. "Proteolytic fragmentation and peptide mapping of human carboxyamidomethylated tracheobronchial mucin."
      Rose M.C., Kaufman B., Martin B.M.
      J. Biol. Chem. 264:8193-8199(1989) [PubMed] [Europe PMC] [Abstract]
      Tissue: Tracheobronchial mucosa.
    5. "Genomic organization of the 3'-region of the human MUC5AC mucin gene: additional evidence for a common ancestral gene for the 11p15.5 mucin gene family."
      Buisine M.P., Desseyn J.-L., Porchet N., Degand P., Laine A., Aubert J.-P.
      Biochem. J. 332:729-738(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 3950-5030, VARIANT PRO-4897.
      Tissue: Placenta and Trachea.
    6. "Cloning and analysis of cDNA encoding a major airway glycoprotein, human tracheobronchial mucin (MUC5)."
      Meerzaman D., Charles P., Daskal E., Polymeropoulos M.H., Martin B.M., Rose M.C.
      J. Biol. Chem. 269:12932-12939(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3990-5030, PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
      Tissue: Nasal polyp.
    7. "Characterization of a mucin cDNA clone isolated from HT-29 mucus secreting cells: the 3' end of MUC5AC?"
      Lesuffleur T., Roche F., Hill A.S., Lacasa M., Fox M., Swallow D.M., Zweibaum A., Real F.X.
      J. Biol. Chem. 270:13665-13673(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4081-5030.
    8. "Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin."
      Lidell M.E., Hansson G.C.
      Biochem. J. 399:121-129(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4303-4312, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-4302.
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4457-5030, VARIANT PRO-4897.
      Tissue: Colon.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4569-5030.
      Tissue: Stomach.
    11. Cited for: STRUCTURE OF O-LINKED CARBOHYDRATES.
    12. "The MUC5AC glycoprotein is the primary receptor for Helicobacter pylori in the human stomach."
      Van de Bovenkamp J.H., Mahdavi J., Korteland-Van Male A.M., Bueller H.A., Einerhand A.W., Boren T., Dekker J.
      Helicobacter 8:521-532(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS LEWIS B BLOOD GROUP ANTIGEN, TISSUE SPECIFICITY, INTERACTION WITH HELICOBACTER PYLORI.
    13. "C-Mannosylation of MUC5AC and MUC5B Cys subdomains."
      Perez-Vilar J., Randell S.H., Boucher R.C.
      Glycobiology 14:325-337(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT TRP-2122, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-2122.

    Entry informationi

    Entry nameiMUC5A_HUMAN
    AccessioniPrimary (citable) accession number: P98088
    Secondary accession number(s): O60460
    , O76065, Q13792, Q14425, Q658Q1, Q7M4S5, Q8N4M9, Q8WWQ3, Q8WWQ4, Q8WWQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3