MUC5B_CHICK
ID MUC5B_CHICK Reviewed; 2108 AA.
AC Q98UI9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Mucin-5B;
DE AltName: Full=Ovomucin, alpha-subunit;
DE Flags: Precursor;
GN Name=MUC5B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=15620212; DOI=10.1080/10425170410001723921;
RA Watanabe K., Shimoyamada M., Onizuka T., Akiyama H., Niwa M., Ido T.,
RA Tsuge Y.;
RT "Amino acid sequence of alpha-subunit in hen egg white ovomucin deduced
RT from cloned cDNA.";
RL DNA Seq. 15:251-261(2004).
RN [2]
RP STRUCTURE OF CARBOHYDRATES, FUNCTION, AND SUBUNIT.
RX PubMed=5119791; DOI=10.1042/bj1210537;
RA Robinson D.S., Monsey J.B.;
RT "Studies on the composition of egg-white ovomucin.";
RL Biochem. J. 121:537-547(1971).
RN [3]
RP GLYCOSYLATION AT ASN-381; ASN-528; ASN-599; ASN-680; ASN-772; ASN-855;
RP ASN-1036; ASN-1219; ASN-1371; ASN-1452; ASN-1567; ASN-1639; ASN-1792;
RP ASN-1807; ASN-1841 AND ASN-1964, LACK OF GLYCOSYLATION AT ASN-69 AND
RP ASN-673, IDENTIFICATION BY MASS SPECTROMETRY, AND STRUCTURE OF
RP CARBOHYDRATES.
RX PubMed=21484392; DOI=10.1007/s10719-011-9328-3;
RA Offengenden M., Fentabil M.A., Wu J.;
RT "N-glycosylation of ovomucin from hen egg white.";
RL Glycoconj. J. 28:113-123(2011).
CC -!- FUNCTION: Ovomucin, the glycoprotein responsible for the gel properties
CC of egg white, is composed for 2 subunits, alpha-ovomucin/MUC5B and
CC beta-ovomucin/MUC6. {ECO:0000269|PubMed:5119791}.
CC -!- SUBUNIT: Multimer; disulfide-linked. {ECO:0000269|PubMed:5119791}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated. Complex glycosylation with bisecting N-
CC acetylglucosamine. Contains mainly N-acetylglucosamine (3.1-8.5%),
CC mannose (2.9-4.6%), a small amount of galactose (1.1-4.35) and sialic
CC acid (0.3-1.3%). Most abundant glycan is composed of a GlcNAc(2)Man(3)
CC core, a bisecting GlcNAc and another 3 GlcNAc antannae located on the
CC mannoses of the core. Site Asn-1639 exists both in glycosylated and
CC non-glycosylated forms. {ECO:0000269|PubMed:21484392}.
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DR EMBL; AB046524; BAB21488.1; -; mRNA.
DR RefSeq; NP_989992.1; NM_204661.1.
DR AlphaFoldDB; Q98UI9; -.
DR SMR; Q98UI9; -.
DR STRING; 9031.ENSGALP00000010852; -.
DR Allergome; 2741; Gal d Ovomucin.
DR iPTMnet; Q98UI9; -.
DR PaxDb; Q98UI9; -.
DR PRIDE; Q98UI9; -.
DR GeneID; 395381; -.
DR KEGG; gga:395381; -.
DR CTD; 395381; -.
DR VEuPathDB; HostDB:geneid_395381; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q98UI9; -.
DR PhylomeDB; Q98UI9; -.
DR PRO; PR:Q98UI9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0046790; F:virion binding; IDA:AgBase.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:AgBase.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:AgBase.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:AgBase.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF00094; VWD; 4.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF57567; SSF57567; 5.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..2108
FT /note="Mucin-5B"
FT /id="PRO_5000049585"
FT DOMAIN 36..203
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 304..360
FT /note="TIL 1"
FT DOMAIN 398..570
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 666..723
FT /note="TIL 2"
FT DOMAIN 782..825
FT /note="TIL 3"
FT DOMAIN 825..897
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 863..1033
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1429..1613
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1761..1832
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1870..1937
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2010..2104
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 196..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 69
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:21484392"
FT SITE 673
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1219
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1371
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1452
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1567
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1639
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1792
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1807
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1841
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 1964
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT DISULFID 38..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 60..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 400..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 422..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 443..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 865..997
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 887..1032
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 896..994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 914..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1431..1573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1453..1612
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1477..1485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2010..2066
FT /evidence="ECO:0000250"
FT DISULFID 2031..2080
FT /evidence="ECO:0000250"
FT DISULFID 2042..2096
FT /evidence="ECO:0000250"
FT DISULFID 2046..2098
FT /evidence="ECO:0000250"
SQ SEQUENCE 2108 AA; 233553 MW; 68B887CB781E6539 CRC64;
MEIKKERSFW IFCLIWSFCK GKEPVQIVQV STVGRSECTT WGNFHFHTFD HVKFTFPGTC
TYVFASHCND SYQDFNIKIR RSDKNSHLIY FTVTTDGVIL EVKETGITVN GNQIPLPFSL
KSILIEDTCA YFQVTSKLGL TLKWNWADTL LLDLEETYKE KICGLCGNYD GNKKNDLILD
GYKMHPRQFG NFHKVEDPSE KCPDVRPDDH TGRHPTEDDN RCSKYKKMCK KLLSRFGNCP
KVVAFDDYVA TCTEDMCNCV VNSSQSDLVS SCICSTLNQY SRDCVLSKGD PGEWRTKELC
YQECPSNMEY MECGNSCADT CADPERSKIC KAPCTDGCFC PPGTILDDLG GKKCVPRDSC
PCMFQGKVYS SGGTYSTPCQ NCTCKGGHWS CISLPCSGSC SIDGGFHIKT FDNKKFNFHG
NCHYVLAKNT DDTFVVIGEI IQCGTSKTMT CLKNVLVTLG RTTIKICSCG SIYMNNFIVK
LPVSKDGITI FRPSTFFIKI LSSAGVQIRV QMKPVMQLSI TVDHSYQNRT SGLCGNFNNI
QTDDFRTATG AVEDSAAAFG NSWKTRASCF DVEDSFEDPC SNSVDKEKFA QHWCALLSNT
SSTFAACHSV VDPSVYIKRC MYDTCNAEKS EVALCSVLST YSRDCAAAGM TLKGWRQGIC
DPSEECPETM VYNYSVKYCN QSCRSLDEPD PLCKVQIAPM EGCGCPEGTY LNDEEECVTP
DDCPCYYKGK IVQPGNSFQE DKLLCKCIQG RLDCIGETVL VKDCPAPMYY FNCSSAGPGA
IGSECQKSCK TQDMHCYVTE CVSGCMCPDG LVLDGSGGCI PKDQCPCVHG GHFYKPGETI
RVDCNTCTCN KRQWNCTDNP CKGTCTVYGN GHYMSFDGEK FDFLGDCDYI LAQDFCPNNM
DAGTFRIVIQ NNACGKSLSI CSLKITLIFE SSEIRLLEGR IQEIATDPGA EKNYKVDLRG
GYIVIETTQG MSFMWDQKTT VVVHVTPSFQ GKVCGLCGDF DGRSRNDFTT RGQSVEMSIQ
EFGNSWKITS TCSNINMTDL CADQPFKSAL GQKHCSIIKS SVFEACHSKV NPIPYYESCV
SDFCGCDSVG DCECFCTSVA AYARSCSTAG VCINWRTPAI CPVFCDYYNP PDKHEWFYKP
CGAPCLKTCR NPQGKCGNIL YSLEGCYPEC SPDKPYFDEE RRECVSLPDC TSCNPEEKLC
TEDSKDCLCC YNGKTYPLNE TIYSQTEGTK CGNAFCGPNG MIIETFIPCS TLSVPAQEQL
MQPVTSAPLL STEATPCFCT DNGQLIQMGE NVSLPMNISG HCAYSICNAS CQIELIWAEC
KVVQTEALET CEPNSEACPP TAAPNATSLV PATALAPMSD CLGLIPPRKF NESWDFGNCQ
IATCLGEENN IKLSSITCPP QQLKLCVNGF PFMKHHDETG CCEVFECQCI CSGWGNEHYV
TFDGTYYHFK ENCTYVLVEL IQPSSEKFWI HIDNYYCGAA DGAICSMSLL IFHSNSLVIL
TQAKEHGKGT NLVLFNDKKV VPDISKNGIR ITSSGLYIIV EIPELEVYVS YSRLAFYIKL
PFGKYYNNTM GLCGTCTNQK SDDARKRNGE VTDSFKEMAL DWKAPVSTNR YCNPGISEPV
KIENYQHCEP SELCKIIWNL TECHRVVPPQ PYYEACVASR CSQQHPSTEC QSMQTYAALC
GLHGICVDWR GQTNGQCEAT CARDQVYKPC GEAKRNTCFS REVIVDTLLS RNNTPVFVEG
CYCPDGNILL NEHDGICVSV CGCTAQDGSV KKPREAWEHD CQYCTCDEET LNISCFPRPC
AKSPPINCTK EGFVRKIKPR LDDPCCTETV CECDIKTCII NKTACDLGFQ PVVAISEDGC
CPIFSCIPKG VCVSEGVEFK PGAVVPKSSC EDCVCTDEQD AVTGTNRIQC VPVKCQTTCQ
QGFRYVEKEG QCCSQCQQVA CVANFPFGSV TIEVGKSYKA PYDNCTQYTC TESGGQFSLT
STVKVCLPFE ESNCVPGTVD VTSDGCCKTC IDLPHKCKRS MKEQYIVHKH CKSAAPVPVP
FCEGTCSTYS VYSFENNEME HKCICCHEKK SHVEKVELVC SEHKTLKFSY VHVDECGCVE
TKCPMRRT
