MUC6_CHICK
ID MUC6_CHICK Reviewed; 1185 AA.
AC F1NBL0; Q6L608;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Mucin-6;
DE AltName: Full=Ovomucin, beta-subunit;
DE Flags: Fragment;
GN Name=MUC6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-839.
RC TISSUE=Oviduct;
RA Watanabe K., Shimoyamada M., Onizuka T., Akiyama H.;
RT "Partial amino acid Sequence of beta-subunit in hen egg white ovomucin
RT deduced from cloned cDNA.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP GLYCOSYLATION AT ASN-223 AND ASN-930, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 {ECO:0000250}.
CC -!- PTM: N-glycosylated with N-acetylglucosamine (6.7%), N-
CC acetylgalactosamine (0.6%), galactose (1.8%), mannose (4.6%), N-
CC acetylneuraminic acid (1.0%) and sulfate-containing glycans (0.7%).
CC {ECO:0000269|PubMed:21484392}.
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DR EMBL; AADN02030346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB180913; BAD22545.1; -; mRNA.
DR AlphaFoldDB; F1NBL0; -.
DR SMR; F1NBL0; -.
DR STRING; 9031.ENSGALP00000032057; -.
DR Allergome; 2741; Gal d Ovomucin.
DR iPTMnet; F1NBL0; -.
DR PaxDb; F1NBL0; -.
DR VEuPathDB; HostDB:geneid_414878; -.
DR VEuPathDB; HostDB:LOC121113279; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; F1NBL0; -.
DR OrthoDB; 12226at2759; -.
DR PhylomeDB; F1NBL0; -.
DR TreeFam; TF300299; -.
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:0099512; C:supramolecular fiber; IDA:AgBase.
DR GO; GO:0003823; F:antigen binding; 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 GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:AgBase.
DR InterPro; IPR030124; MUC6.
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 PANTHER; PTHR11339:SF264; PTHR11339:SF264; 1.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF00094; VWD; 3.
DR SMART; SM00832; C8; 3.
DR SMART; SM00215; VWC_out; 1.
DR SMART; SM00216; VWD; 3.
DR SUPFAM; SSF57567; SSF57567; 3.
DR PROSITE; PS51233; VWFD; 3.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted.
FT CHAIN <1..1185
FT /note="Mucin-6"
FT /id="PRO_0000412756"
FT DOMAIN <1..169
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 257..312
FT /note="TIL 1"
FT DOMAIN 350..534
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 619..676
FT /note="TIL 2"
FT DOMAIN 737..782
FT /note="TIL 3"
FT DOMAIN 821..993
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1160..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:21484392"
FT DISULFID 1..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 23..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 352..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 374..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 823..957
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 845..992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 854..954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 872..879
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 13..16
FT /note="DKYQ -> PTRP (in Ref. 2; BAD22545)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1185 AA; 132217 MW; AE19DF5A5B290D7E CRC64;
CSTWGGGHFS TFDKYQYDFT GTCNYIFATV CDESSPDFNI QFRRGLDKKI ARIIIELGPS
VIIVEKDSIS VRSVGVIKLP YASNGIQIAP YGRSVRLVAK LMEMELVVMW NNEDYLMVLT
EKKYMGKTCG MCGNYDGYEL NDFVSEGKLL DTYKFAALQK MDDPSEICLS EEISIPAIPH
KKYAVICSQL LNLVSPTCSV PKDGFVTRCQ LDMQDCSEPG QKNCTCSTLS EYSRQCAMSH
QVVFNWRTEN FCSVGKCSAN QIYEECGSPC IKTCSNPEYS CSSHCTYGCF CPEGTVLDDI
SKNRTCVHLE QCPCTLNGET YAPGDTMKAA CRTCKCTMGQ WNCKELPCPG RCSLEGGSFV
TTFDSRSYRF HGVCTYILMK SSSLPHNGTL MAIYEKSGYS HSETSLSAII YLSTKDKIVI
SQNELLTDDD ELKRLPYKSG DITIFKQSSM FIQMHTEFGL ELVVQTSPVF QAYVKVSAQF
QGRTLGLCGN YNGDTTDDFM TSMDITEGTA SLFVDSWRAG NCLPAMERET DPCALSQLNK
ISAETHCSIL TKKGTVFETC HAVVNPTPFY KRCVYQACNY EETFPYICSA LGSYARTCSS
MGLILENWRN SMDNCTITCT GNQTFSYNTQ ACERTCLSLS NPTLECHPTD IPIEGCNCPK
GMYLNHKNEC VRKSHCPCYL EDRKYILPDQ STMTGGITCY CVNGRLSCTG KLQNPAESCK
APKKYISCSD SLENKYGATC APTCQMLATG IECIPTKCES GCVCADGLYE NLDGRCVPPE
ECPCEYGGLS YGKGEQIQTE CEICTCRKGK WKCVQKSRCS STCNLYGEGH ITTFDGQRFV
FDGNCEYILA MDGCNVNRPL SSFKIVTENV ICGKSGVTCS RSISIYLGNL TIILRDETYS
ISGKNLQVKY NVKKNALHLM FDIIIPGKYN MTLIWNKHMN FFIKISRETQ ETICGLCGNY
NGNMKDDFET RSKYVASNEL EFVNSWKENP LCGDVYFVVD PCSKNPYRKA WAEKTCSIIN
SQVFSACHNK VNRMPYYEAC VRDSCGCDIG GDCECMCDAI AVYAMACLDK GICIDWRTPE
FCPVYCEYYN SHRKTGSGGA YSYGSSVNCT WHYRPCNCPN QYYKYVNIEG CYNCSHDEYF
DYEKEKCMPC AMQPTSVTLP TATQPTSPST SSASTVLTET TNPPV
