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 24-JAN-2024, entry version 59. 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}. 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; AADN02030346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB180913; BAD22545.1; -; mRNA. DR AlphaFoldDB; F1NBL0; -. DR SMR; F1NBL0; -. DR STRING; 9031.ENSGALP00000050462; -. DR Allergome; 2741; Gal d Ovomucin. DR GlyCosmos; F1NBL0; 2 sites, No reported glycans. DR iPTMnet; F1NBL0; -. DR PaxDb; 9031-ENSGALP00000032057; -. DR VEuPathDB; HostDB:geneid_414878; -. DR VEuPathDB; HostDB:LOC121113279; -. DR eggNOG; KOG1216; Eukaryota. DR InParanoid; F1NBL0; -. DR PhylomeDB; F1NBL0; -. DR TreeFam; TF300299; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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:0030308; P:negative regulation of cell growth; IMP:AgBase. DR CDD; cd19941; TIL; 3. DR Gene3D; 2.10.25.10; Laminin; 3. DR InterPro; IPR036084; Ser_inhib-like_sf. DR InterPro; IPR002919; TIL_dom. DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom. DR InterPro; IPR001007; VWF_dom. DR InterPro; IPR001846; VWF_type-D. DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1. DR PANTHER; PTHR11339:SF264; MUCIN-6; 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; Serine protease inhibitors; 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 //