ID A0A2Y9JS25_ENHLU Unreviewed; 491 AA.
AC A0A2Y9JS25;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Myocilin {ECO:0000256|ARBA:ARBA00017216};
GN Name=LOC111150631 {ECO:0000313|RefSeq:XP_022363827.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022363827.1};
RN [1] {ECO:0000313|RefSeq:XP_022363827.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022363827.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004294}. Rough endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004427}. Secreted, extracellular exosome
CC {ECO:0000256|ARBA:ARBA00004550}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00446}.
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DR RefSeq; XP_022363827.1; XM_022508119.1.
DR AlphaFoldDB; A0A2Y9JS25; -.
DR STRING; 391180.A0A2Y9JS25; -.
DR KEGG; elk:111150631; -.
DR OrthoDB; 2876896at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR23192:SF33; MYOCILIN; 1.
DR PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..491
FT /note="Myocilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016175727"
FT DOMAIN 231..490
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT REGION 145..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54316 MW; FD80E25FCF6E0328 CRC64;
MAAVQLLLLA CLVWAFEART AQLRKADDRS GHCQYTFSVA SPTEPSCPEQ GQAASAIRDL
QRDSSAQRAD LEAAKARLSS LEGLLRRLTA GQAAGPSDGQ EGPQGELDAL RRDREHLETQ
VRELEVAYGN LLRDKAALEE EKRRLGQEND DLAQTLESSS QEVARLRRGQ CTQAHSSSQD
APPGSGEEVP KWNMETANFQ ELKSELTEVP ASRILKESPS GHPENEEGDP GCGELVWVGE
PLTLRRAETA AGKYGVWMRD PKPRPPHTAE TTWRVDTVGT DVRQVFEYDR AAQFLQGHPS
RVHVLPRPLE STGAVVYAGS LYFQAAGSAT LVRYDLASET VRAERELPGA GFRGQFPYSW
GGYTDIDLAV DETGLWVIYS TRAARGAIVL SKLSPESLAP ERTWETNIRK RAVANAFLLC
GRLYTVSSYS SPEAAVNFAY DPATGRSKAL RVPLRVRYGY CSALDYNPRE RRLFAWDNFH
MVAYDVRLSR G
//
