P98088 (MUC5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MUC5AC
Synonyms:	MUC5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	5030 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Multimeric. Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD). Ref.12
Subcellular location	Secreted Ref.13.
Tissue specificity	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. Ref.6 Ref.12
Domain	The cysteine residues in the Cys-rich subdomain repeats are not involved in disulfide bonding.
Post-translational modification	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. Ref.11 Ref.13 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.
Sequence similarities	Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 2 VWFC domains. Contains 4 VWFD domains.
Sequence caution	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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome cellular protein metabolic process Traceable author statement. Source: Reactome extracellular fibril organization Inferred from direct assay PubMed 10611155. Source: MGI post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 19199708. Source: UniProt fibril Inferred from direct assay PubMed 14749330. Source: MGI
Molecular_function	extracellular matrix structural constituent Traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 5030	5003	Mucin-5AC		PRO_0000158957
Regions
	Domain	80 – 281	202	VWFD 1
	Domain	433 – 647	215	VWFD 2
	Domain	902 – 1109	208	VWFD 3
	Repeat	1383 – 1481	99	Cys-rich subdomain 1
	Repeat	1577 – 1677	101	Cys-rich subdomain 2
	Repeat	1743 – 1847	105	Cys-rich subdomain 3
	Repeat	1950 – 2050	101	Cys-rich subdomain 4
	Repeat	2116 – 2220	105	Cys-rich subdomain 5
	Repeat	2646 – 2750	105	Cys-rich subdomain 6
	Repeat	2944 – 3084	141	Cys-rich subdomain 7
	Repeat	3377 – 3481	105	Cys-rich subdomain 8
	Repeat	4003 – 4107	105	Cys-rich subdomain 9
	Domain	4296 – 4507	212	VWFD 4
	Domain	4652 – 4721	70	VWFC 1
	Domain	4757 – 4824	68	VWFC 2
	Domain	4908 – 4996	89	CTCK
	Region	1383 – 4107	2725	9 X Cys-rich subdomain repeats
	Region	2257 – 2624	368	46 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P
	Region	2787 – 2922	136	17 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P
	Region	3085 – 3355	271	34 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P
	Region	3517 – 3971	455	58 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P
	Motif	1193 – 1195	3	Cell attachment site Potential
	Compositional bias	4896 – 4901	6	Poly-Pro
Sites
	Site	4302 – 4303	2	Cleavage
Amino acid modifications
	Glycosylation	205	1	N-linked (GlcNAc...) Potential
	Glycosylation	258	1	N-linked (GlcNAc...) Potential
	Glycosylation	415	1	N-linked (GlcNAc...) Potential
	Glycosylation	524	1	N-linked (GlcNAc...) Potential
	Glycosylation	1308	1	N-linked (GlcNAc...) Potential
	Glycosylation	1389	1	C-linked (Man) Probable
	Glycosylation	1584	1	C-linked (Man) Probable
	Glycosylation	1749	1	C-linked (Man) Probable
	Glycosylation	1957	1	C-linked (Man) Probable
	Glycosylation	2122	1	C-linked (Man) Ref.13
	Glycosylation	2652	1	C-linked (Man) Probable
	Glycosylation	2950	1	C-linked (Man) Probable
	Glycosylation	3198	1	N-linked (GlcNAc...) Potential
	Glycosylation	3383	1	C-linked (Man) Probable
	Glycosylation	4009	1	C-linked (Man) Probable
	Glycosylation	4245	1	N-linked (GlcNAc...) Potential
	Glycosylation	4318	1	N-linked (GlcNAc...) Potential
	Glycosylation	4433	1	N-linked (GlcNAc...) Potential
	Glycosylation	4469	1	N-linked (GlcNAc...) Potential
	Glycosylation	4612	1	N-linked (GlcNAc...) Potential
	Glycosylation	4723	1	N-linked (GlcNAc...) Potential
	Glycosylation	4753	1	N-linked (GlcNAc...) Potential
	Glycosylation	4762	1	N-linked (GlcNAc...) Potential
	Glycosylation	4831	1	N-linked (GlcNAc...) Potential
	Glycosylation	4904	1	N-linked (GlcNAc...) Potential
	Glycosylation	4967	1	N-linked (GlcNAc...) Potential
	Disulfide bond	103 ↔ 111		By similarity
	Disulfide bond	456 ↔ 464		By similarity
	Disulfide bond	4908 ↔ 4958		By similarity
	Disulfide bond	4922 ↔ 4972		By similarity
	Disulfide bond	4933 ↔ 4988		By similarity
	Disulfide bond	4937 ↔ 4990		By similarity
	Disulfide bond	? ↔ 4995		By similarity
Natural variations
	Natural variant	4897	1	L → P. Ref.5 Ref.9 Corresponds to variant rs1132436 [ dbSNP | Ensembl ].		VAR_036832
Experimental info
	Mutagenesis	2122	1	W → A: No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum. Ref.13
	Mutagenesis	4302	1	D → A or E: Abolishes cleavage. Ref.8
	Sequence conflict	221	1	S → R in AAC15950. Ref.2
	Sequence conflict	432	1	D → G in AAC15950. Ref.2
	Sequence conflict	549	1	P → L in AAC15950. Ref.2
	Sequence conflict	658	1	V → M in AAC15950. Ref.2
	Sequence conflict	702	1	T → I in AAC15950. Ref.2
	Sequence conflict	716	1	T → A in AAC15950. Ref.2
	Sequence conflict	817 – 818	2	GD → RG in AAC15950. Ref.2
	Sequence conflict	869	1	E → K in AAC15950. Ref.2
	Sequence conflict	978	1	G → R in AAC15950. Ref.2
	Sequence conflict	996	1	Q → R in AAC15950. Ref.2
	Sequence conflict	1803	1	E → N AA sequence Ref.4
	Sequence conflict	2176	1	E → N AA sequence Ref.4
	Sequence conflict	3004	1	E → N AA sequence Ref.4
	Sequence conflict	3990 – 3991	2	VS → HE in AAA18431. Ref.6
	Sequence conflict	4203	1	P → R in CAA88307. Ref.7
	Sequence conflict	4260 – 4262	3	SPR → RPP in AAA18431. Ref.6
	Sequence conflict	4275	1	G → A in AAA18431. Ref.6
	Sequence conflict	4389	1	G → A in CAA88307. Ref.7
	Sequence conflict	4457 – 4460	4	VVAS → HASA in AAH33831. Ref.9
	Sequence conflict	4524	1	H → Q in CAA04737. Ref.5
	Sequence conflict	4524	1	H → Q in CAA04738. Ref.5
	Sequence conflict	4569	1	A → R in AAA18431. Ref.6
	Sequence conflict	4621	1	R → P in CAA88307. Ref.7
	Sequence conflict	4640	1	S → T in CAA04737. Ref.5
	Sequence conflict	4640	1	S → T in CAA04738. Ref.5
	Sequence conflict	4732	1	G → R in AAA18431. Ref.6
	Sequence conflict	4739	1	A → R in AAA18431. Ref.6
	Sequence conflict	4809	1	G → R in AAA18431. Ref.6
	Sequence conflict	4922	1	C → S in AAA18431. Ref.6
	Non-adjacent residues	2448 – 2449	2
	Non-adjacent residues	3797 – 3798	2

Sequences

	Sequence		Length	Mass (Da)
	P98088 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: 00523008FF20ACAB	FASTA	5,030	526,608
	10 20 30 40 50 60 MSVGRRKLAL LWALALALAC TRHTGHAQDG SSESSYKHHP ALSPIARGPS GVPLRGATVF 70 80 90 100 110 120 PSLRTIPVVR ASNPAHNGRV CSTWGSFHYK TFDGDVFRFP GLCNYVFSEH CGAAYEDFNI 130 140 150 160 170 180 QLRRSQESAA PTLSRVLMKV DGVVIQLTKG SVLVNGHPVL LPFSQSGVLI QQSSSYTKVE 190 200 210 220 230 240 ARLGLVLMWN HDDSLLLELD TKYANKTCGL CGDFNGMPVV SELLSHNTKL TPMEFGNLQK 250 260 270 280 290 300 MDDPTEQCQD PVPEPPRNCS TGFGICEELL HGQLFSGCVA LVDVGSYLEA CRQDLCFCED 310 320 330 340 350 360 TDLLSCVCHT LAEYSRQCTH AGGLPQDWRG PDFCPQKCPN NMQYHECRSP CADTCSNQEH 370 380 390 400 410 420 SRACEDHCVA GCFCPEGTVL DDIGQTGCVP VSKCACVYNG AAYAPGATYS TDCTNCTCSG 430 440 450 460 470 480 GRWSCQEVPC PDTCSVLGGA HFSTFDGKQY TVHGDCSYVL TKPCDSSAFT VLAELRRCGL 490 500 510 520 530 540 TDSETCLKSV TLSLDGAQTV VVIKASGEVF LNQIYTQLPI SAANVTIFRP STFFIIAQTS 550 560 570 580 590 600 LGLQLNLQPV PTMQLFMQLA PKLRGQTCGL CGNFNSIQAD DFRTLSGVVE ATAAAFFNTF 610 620 630 640 650 660 KTQAACPNIR NSFEDPCSLS VENEKYAQHW CSQLTDADGP FGRCHAAVKP GTYYSNCVFD 670 680 690 700 710 720 TCNCERSEDC LCAALSSYVH ACAAKGVQLG GWRDGVCTKP MTTCPKSMTY HYHVSTCQPT 730 740 750 760 770 780 CRSLSEGDIT CSVGFIPVDG CICPKGTFLD DTGKCVQASN CPCYHRGSMI PNGESVHDSG 790 800 810 820 830 840 AICTCTHGKL SCIGGQAPAP VCAAPMVFFD CRNATPGDTG AGCQKSCHTL DMTCYSPQCV 850 860 870 880 890 900 PGCVCPDGLV ADGEGGCITA EDCPCVHNEA SYRAGQTIRV GCNTCTCDSR MWRCTDDPCL 910 920 930 940 950 960 ATCAVYGDGH YLTFDGQSYS FNGDCEYTLV QNHCGGKDST QDSFRVVTEN VPCGTTGTTC 970 980 990 1000 1010 1020 SKAIKIFLGG FELKLSHGKV EVIGTDESQE VPYTIQQMGI YLVVDTDIGL VLLWDKKTSI 1030 1040 1050 1060 1070 1080 FINLSPEFKG RVCGLCGNFD DIAVNDFATR SRSVVGDVLE FGNSWKLSPS CPDALAPKDP 1090 1100 1110 1120 1130 1140 CTANPFRKSW AQKQCSILHG PTFAACHAHV EPARYYEACV NDACACDSGG DCECFCTAVA 1150 1160 1170 1180 1190 1200 AYAQACHEVG LCVCLRTPSI CPLFCDYYNP EGQCEWHYQP CGVPCLRTCR NPRGDCLRDV 1210 1220 1230 1240 1250 1260 RGLEGCYPKC PPEAPIFDED KMQCVATCPT PPLPPRCHVH GKSYRPGAVV PSDKNCQSCL 1270 1280 1290 1300 1310 1320 CTERGVECTY KAEACVCTYN GQRFHPGDVI YHTTDGTGGC ISARCGANGT IERRVYPCSP 1330 1340 1350 1360 1370 1380 TTPVPPTTFS FSTPPLVVSS THTPSNGPSS AHTGPPSSAW PTTAGTSPRT RLPTASASLP 1390 1400 1410 1420 1430 1440 PVCGEKCLWS PWMDVSRPGR GTDSGDFDTL ENLRAHGYRV CESPRSVECR AEDAPGVPLR 1450 1460 1470 1480 1490 1500 ALGQRVQCSP DVGLTCRNRE QASGLCYNYQ IRVQCCTPLP CSTSSSPAQT TPPTTSKTTE 1510 1520 1530 1540 1550 1560 TRASGSSAPS STPGTVSLST ARTTPAPGTA TSVKKTFSTP SPPPVPATST SSMSTTAPGT 1570 1580 1590 1600 1610 1620 SVVSSKPTPT EPSTSSCLQE LCTWTEWIDG SYPAPGINGG DFDTFQNLRD EGYTFCESPR 1630 1640 1650 1660 1670 1680 SVQCRAESFP NTPLADLGQD VICSHTEGLI CLNKNQLPPI CYNYEIRIQC CETVNVCRDI 1690 1700 1710 1720 1730 1740 TRLPKTVATT RPTPHPTGAQ TQTTFTTHMP SASTEQPTAT SRGGPTATSV TQGTHTTLVT 1750 1760 1770 1780 1790 1800 RNCHPRCTWT KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRV QCRAKSHPEV 1810 1820 1830 1840 1850 1860 SIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPRGCHMT STPGSTSSSP 1870 1880 1890 1900 1910 1920 AQTTPSTTSK TTEIQASGSS APSSTPGTVS LSTARTTPAP GTATSVKKTF STPSPPPVPA 1930 1940 1950 1960 1970 1980 TSTSSMSTTA PGTSVVSSKP TPTEPSTSSC LQELCTWTEW IDGSYPAPGI NGGDFDTFQN 1990 2000 2010 2020 2030 2040 LRDEGYTFCE SPRSVQCRAE SFPNTPLGRL GQDVICSHTE GLICLNKNQL PPICYNYEIR 2050 2060 2070 2080 2090 2100 IQCCETVNVC RDITRPPKTV ATTRPTPHPT GAQTQTTFTT HMPSASTEQP TATSRGGPTA 2110 2120 2130 2140 2150 2160 TSVTQGTHTT PVTRNCHPRC TWTTWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI 2170 2180 2190 2200 2210 2220 TRLQCRAKSH PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNIEVR VLCCETPKGC 2230 2240 2250 2260 2270 2280 PVTSTPVTAP STPSGRAISP TQSTSSWQKS RTTTLVTTST TSTPQTSTTY AHTTSTTSAP 2290 2300 2310 2320 2330 2340 TARTTSAPTT STTSVPTTST ISGPKTTPSP VPTTSTTSAA TTSTISAPTT STTSVPGTTP 2350 2360 2370 2380 2390 2400 SPVLTTSTTS APTTRTTSAS PAGTTSGPGN TPSPVPTTST ISAPTTSITS APTTSTTSAP 2410 2420 2430 2440 2450 2460 TSSTTSGPGT TPSPVPTTSI TSAPTTSTTS APTTSTTSAP TTSTTSAPTT STTSAPTTST 2470 2480 2490 2500 2510 2520 TSTPTSSTTS TPQTSTTSAS TTSITSGPGT TPSPVPTTST TSAPTTSTTS AATTSTISAP 2530 2540 2550 2560 2570 2580 TTSTTSAPTT STTSASTASK TSGLGTTPSP IPTTSTTSPP TTSTTSASTA SKTSGPGTTP 2590 2600 2610 2620 2630 2640 SPVPTTSTIF APRTSTTSAS TTSTTPGPGT TPSPVPTTST ASVSKTSTSH VSISKTTHSQ 2650 2660 2670 2680 2690 2700 PVTRDCHLRC TWTKWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI TRLQCRAESH 2710 2720 2730 2740 2750 2760 PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNYEVR VLCCETPKGC PVTSTPVTAP 2770 2780 2790 2800 2810 2820 STPSGRATSP TQSTSSWQKS RTTTLVTTST TSTPQTSTTS APTTSTTSAP TTSTTSAPTT 2830 2840 2850 2860 2870 2880 STTSTPQTSI SSAPTSSTTS APTSSTISAR TTSIISAPTT STTSSPTTST TSATTTSTTS 2890 2900 2910 2920 2930 2940 APTSSTTSTP QTSKTSAATS STTSSSGTTP SPVTTTSTAS VSKTSTSHVS VSKTTHSQPV 2950 2960 2970 2980 2990 3000 TRDCHPRCTW TKWFDVDFPS PGPHGGDKET YNNIIRSGEK ICRRPQEITR LQCRAKSHPE 3010 3020 3030 3040 3050 3060 VSIEHLGQVV QCSREEGLVC RNQDQQGPFK MCLNYEVRVL CCETPKGCPV TSTSVTAPSP 3070 3080 3090 3100 3110 3120 LVGEPPAQTQ STSSWQKSRT TTLVTSSITS TTQTSTTSAP TTSTTPASIP STTSAPTTST 3130 3140 3150 3160 3170 3180 TSAPTTSTTS APTTSTTSTP QTTTSSAPTS STTSAPTTST ISAPTTSTIS APTTSTTSAP 3190 3200 3210 3220 3230 3240 TASTTSAPTS TSSAPTTNTT SAPTTSTTSA PITSTISAPT TSTTSTPQTS TISSPTTSTT 3250 3260 3270 3280 3290 3300 PTPQTSTTSS PTTSTTSAPT TSTTSAPTTS TTSTPQTSIS SAPTSSTTSA PTASTISAPT 3310 3320 3330 3340 3350 3360 TSTTSFHTTS TTSPPTSSTS STPQTSKTSA ATSSTTSGSG TTPSPVPTTS TASVSKTSTS 3370 3380 3390 3400 3410 3420 HVSVSKTTHS QPVTRDCHPR CTWTKWFDVD FPSPGPHGGD KETYNNIIRS GEKICRRPEE 3430 3440 3450 3460 3470 3480 ITRLQCRAES HPEVSIEHLG QVVQCSREEG LVCRNQDQQG PFKMCLNYEV RVLCCETPKG 3490 3500 3510 3520 3530 3540 CPVTSTPVTA PSTPSGRATS PTQSTSSWQK SRTTTLVTTS TTSTPQTSTT SAPTTSTIPA 3550 3560 3570 3580 3590 3600 STPSTTSAPT TSTTSAPTTS TTSAPTHRTT SGPTTSTTLA PTTSTTSAPT TSTNSAPTTS 3610 3620 3630 3640 3650 3660 TISASTTSTI SAPTTSTISS PTSSTTSTPQ TSKTSAATSS TTSGSGTTPS PVPTTSTTSA 3670 3680 3690 3700 3710 3720 STTSTTSAPT TSTTSGPGTT PSPVPSTSIT SAATTSTTSA PTTRTTSAPT SSMTSGPGTT 3730 3740 3750 3760 3770 3780 PSPVPTTSTT SAPTTSTTSG PGTTPSPVPT TSTTSAPITS TTSGPGSTPS PVPTTSTTSA 3790 3800 3810 3820 3830 3840 PTTSTTSAST ASTTSGPTTS TTSASTTSTI SPLTTSTTSA PITSMPSGPG TTPSPVPTTS 3850 3860 3870 3880 3890 3900 TTSAPTTSTT SGPGTTPSPV PTTSTTSAPT TSTTSASTAS TTSGPGTTPS PVPTTSTTSA 3910 3920 3930 3940 3950 3960 PTTSTTSAST ASTTSGPGTS LSPVPTTSTT SAPTTSTTSG PGTTPSPVPT TSTTSAPTTS 3970 3980 3990 4000 4010 4020 TTSGPGTTPS PVPTTSTTPV SKTSTSHLSV SKTTHSQPVT SDCHPLCAWT KWFDVDFPSP 4030 4040 4050 4060 4070 4080 GPHGGDKETY NNIIRSGEKI CRRPEEITRL QCRAESHPEV NIEHLGQVVQ CSREEGLVCR 4090 4100 4110 4120 4130 4140 NQDQQGPFKM CLNYEVRVLC CETPRGCPVT SVTPYGTSPT NALYPSLSTS MVSASVASTS 4150 4160 4170 4180 4190 4200 VASSSVASSS VAYSTQTCFC NVADRLYPAG STIYRHRDLA GHCYYALCSQ DCQVVRGVDS 4210 4220 4230 4240 4250 4260 DCPSTTLPPA PATSPSISTS EPVTELGCPN AVPPRKKGET WATPNCSEAT CEGNNVISLS 4270 4280 4290 4300 4310 4320 PRTCPRVEKP TCANGYPAVK VADQDGCCHH YQCQCVCSGW GDPHYITFDG TYYTFLDNCT 4330 4340 4350 4360 4370 4380 YVLVQQIVPV YGHFRVLVDN YFCGAEDGLS CPRSIILEYH QDRVVLTRKP VHGVMTNEII 4390 4400 4410 4420 4430 4440 FNNKVVSPGF RKNGIVVSRI GVKMYATIPE LGVQVMFSGL IFSVEVPFSK FANNTEGQCG 4450 4460 4470 4480 4490 4500 TCTNDRKDEC RTPRGTVVAS CSEMSGLWNV SIPDQPACHR PHPTPTTVGP TTVGSTTVGP 4510 4520 4530 4540 4550 4560 TTVGSTTVGP TTPPAPCLPS PICHLILSKV FEPCHTVIPP LLFYEGCVFD RCHMTDLDVV 4570 4580 4590 4600 4610 4620 CSSLELYAAL CASHDICIDW RGRTGHMCPF TCPADKVYQP CGPSNPSYCY GNDSASLGAL 4630 4640 4650 4660 4670 4680 REAGPITEGC FCPEGMTLFS TSAQVCVPTG CPRCLGPHGE PVKVGHTVGM DCQECTCEAA 4690 4700 4710 4720 4730 4740 TWTLTCRPKL CPLPPACPLP GFVPVPAAPQ AGQCCPQYSC ACNTSRCPAP VGCPEGARAI 4750 4760 4770 4780 4790 4800 PTYQEGACCP VQNCSWTVCS INGTLYQPGA VVSSSLCETC RCELPGGPPS DAFVVSCETQ 4810 4820 4830 4840 4850 4860 ICNTHCPVGF EYQEQSGQCC GTCVQVACVT NTSKSPAHLF YPGETWSDAG NHCVTHQCEK 4870 4880 4890 4900 4910 4920 HQDGLVVVTT KKACPPLSCS LDEARMSKDG CCRFCPLPPP PYQNQSTCAV YHRSLIIQQQ 4930 4940 4950 4960 4970 4980 GCSSSEPVRL AYCRGNCGDS SSMYSLEGNT VEHRCQCCQE LRTSLRNVTL HCTDGSSRAF 4990 5000 5010 5020 5030 SYTEVEECGC MGRRCPAPGD TQHSEEAEPE PSQEAESGSW ERGVPVSPMH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] Cited for: PROTEIN SEQUENCE OF 1752-1773; 1796-1805; 2125-2146; 2169-2178; 2655-2676; 2697-2708; 2953-2974; 2997-3006; 3386-3407; 3428-3439 AND 4012-4033. 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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4569-5030. Tissue: Stomach.
[11]	"In vivo glycosylation of mucin tandem repeats." Silverman H.S., Parry S., Sutton-Smith M., Burdick M.D., McDermott K., Reid C.J., Batra S.K., Morris H.R., Hollingsworth M.A., Dell A., Harris A. Glycobiology 11:459-471(2001) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Mucin database

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A33811. JE0095.
UniGene	Hs.534332. Hs.558950. Hs.721515.
3D structure databases
ProteinModelPortal	P98088.
SMR	P98088. Positions 336-394, 800-873, 4589-4652, 4903-4994.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
IntAct	P98088. 1 interaction.
Protein family/group databases
MEROPS	I08.951.
PTM databases
UniCarbKB	P98088.
Polymorphism databases
DMDM	160370004.
Proteomic databases
MaxQB	P98088.
PRIDE	P98088.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
GeneCards	GC11P001151.
H-InvDB	HIX0201650.
HGNC	HGNC:7515. MUC5AC.
HPA	CAB002774. CAB009395. HPA040615.
MIM	158373. gene.
neXtProt	NX_P98088.
GenAtlas	Search...
Phylogenomic databases
InParanoid	P98088.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
Genevestigator	P98088.
Family and domain databases
InterPro	IPR006207. Cys_knot_C. IPR002919. TIL_dom. IPR014853. Unchr_dom_Cys-rich. IPR001007. VWF_C. IPR001846. VWF_type-D. IPR025155. WxxW_domain. [Graphical view]
Pfam	PF08742. C8. 4 hits. PF13330. Mucin2_WxxW. 9 hits. PF01826. TIL. 3 hits. PF00094. VWD. 4 hits. [Graphical view]
SMART	SM00832. C8. 4 hits. SM00041. CT. 1 hit. SM00214. VWC. 6 hits. SM00216. VWD. 4 hits. [Graphical view]
SUPFAM	SSF57567. SSF57567. 4 hits.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	125477.
PRO	P98088.
SOURCE	Search...

Entry information

Entry name

MUC5A_HUMAN

Accession

Primary (citable) accession number: P98088
Secondary accession number(s): O60460 , O76065, Q13792, Q14425, Q658Q1, Q7M4S5, Q8N4M9, Q8WWQ3, Q8WWQ4, Q8WWQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	October 23, 2007
Last modified:	May 14, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.