ID I3JNL2_ORENI Unreviewed; 1509 AA.
AC I3JNL2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Mucin 2, oligomeric mucus/gel-forming {ECO:0008006|Google:ProtNLM};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000010456.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000010456.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00039}.
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DR STRING; 8128.ENSONIP00000010456; -.
DR Ensembl; ENSONIT00000010465.2; ENSONIP00000010456.2; ENSONIG00000008311.2.
DR GeneTree; ENSGT00940000163235; -.
DR HOGENOM; CLU_008015_0_0_1; -.
DR InParanoid; I3JNL2; -.
DR OMA; VHVIEVN; -.
DR Proteomes; UP000005207; Linkage group LG1.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR018245; Gonadotropin_bsu_CS.
DR InterPro; IPR036084; Ser_inhib-like_sf.
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:SF398; MUCIN-2-LIKE-RELATED; 1.
DR Pfam; PF08742; C8; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00832; C8; 1.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 3.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00039}; Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 786..964
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1116..1184
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1268..1329
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1401..1496
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1423..1472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 1434..1488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 1438..1490
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 1509 AA; 157666 MW; E2A676682353BFF5 CRC64;
MTTKTPKIVT TGPTTFSTTA IVETTTTVPH VETTGQGSTT VTSKPSVSTE ITSGPFTTTK
GTAATPTETT AFESTTATIM TTKTPKIVTS GPTTSSTTAV VETTTTVPHV ETTGQGSTTV
TSKPSVSTEI TSGPFTTTKG TAATPAQTTA FESTTATIMT TKTPKIVTTG PTTSSTTAIV
ETTTTVPHVE TTGQGSTTVT SKPSVSTEIT SGPFTTTKGT VATPAQTTAF ESTTATVMTT
KTPKIVTSGP TTSSVTAVVE TTTTVPNVKT TGQGSTTVTS KPSVSTEITS GPFTTTKGTA
ATPTETTAFE STTATTVPHV ETTAQGSTTV TSKPSVSTEI TSGPFTTTKG TAATPAQTTA
FESTTATVMT TKTPKIVTSG PTTSSTTAVV EITSTVPNIK TTGQGSTTVT SKPSVSTEIT
SGPFTTTEGT AATPTETTAF ESTTATIMTT KTPKLVTTGP TTSSTTAFVE STTTVPHVET
TGQGSTTVTS KPSVSTEITS GPFTTTEGTA PTPAQTTAFE STTATIMTTK TPKIVTTGPT
TSSTTAASTL AVVTGSSFSS TVITNPSVLN TTILPSTSRG TTSIAPITET LPGSTTVYTT
SVNPSVTTTT VASPSPLNTT STLCVCIVNG ASHHAGDLVY NVTDGLGWCY AAICNASCEI
ETQSSPCPVT PSVPTTAHST TTVFSTTTKA TISSSVPLTT TIPASFTSST SITSSTQNAC
NDVYPPRQNG ESWDAGNCTT ATCINGKIIM MPTVCPTMQQ PICTNGRSAA KISDDDGCCP
HYECRCVCSI WCGSHYLTFD GESYNFNENC SYYLVKEIIA KYNLTIVVNR DCDPSNSTFC
PKALTVAYKS FKVVLTQLTS SGVSTNVVFV NQQKIYPAYS NSVLHITSTD IITTLELQDI
SAKIVYSGSS FSIDLPYSLF EGNTEGQCGT CDNSQSNECR SPNGQVGSCS DTAGEWQVPD
TPCVIPTTPP TPRTTSNPPH STPPVCKPAI CDLLTSSLFA PCHTVVPPGP FVTSCVFDNC
NLGKNSCCSL EAYATECSNE GICIDWRNAT NGLCEHKCPS NKVYMPCGPS VEPTCNNGYN
MAYQTAASSN DTKEGCFCPH GTTLFNTVHD ICVDTCACVG PDGKPKQLGE TWTSDCQTCV
CDKDSMSVQC EPVQCQSVQR PNCSEPGQQL VNNTVNCCTT QSCECNINLC PAPPTCLPGF
QLSITNGTCC LSYKCVPKGV CVYNMTEYKP GAKIPTPDTL SEPPLEAPEA QSMAEQPSVT
TTAPSGAGET STMSESFTPG PCQECYCGPE MDPVTKLNVI TCEPVICNKN CSAGYEYQTE
PGKCCGTCVQ TDCIFTTTDN VTVHVIEVNS SYIPPNNKCV QYTCEKLNGQ LVTKETKTTC
PPFNPLDCEP GTETTDANGC CKTCNISLCK TQKEQRIIEL NNCKSAQPVN ITYCAGHCDS
FSMYSMAANT MVHNCECCQE ATTSVEQVEL TCADGSKLQH SYTMAQSCQC IKTECVEGTT
PKPQRRRRR
//
