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Database: UniProt
Entry: A0A2K6GWE1_PROCO
LinkDB: A0A2K6GWE1_PROCO
Original site: A0A2K6GWE1_PROCO 
ID   A0A2K6GWE1_PROCO        Unreviewed;       594 AA.
AC   A0A2K6GWE1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Multiple EGF like domains 9 {ECO:0000313|Ensembl:ENSPCOP00000030494.1};
GN   Name=MEGF9 {ECO:0000313|Ensembl:ENSPCOP00000030494.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000030494.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000030494.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   RefSeq; XP_012519901.1; XM_012664447.1.
DR   AlphaFoldDB; A0A2K6GWE1; -.
DR   STRING; 379532.ENSPCOP00000030494; -.
DR   Ensembl; ENSPCOT00000041442.1; ENSPCOP00000030494.1; ENSPCOG00000027969.1.
DR   GeneID; 105826459; -.
DR   KEGG; pcoq:105826459; -.
DR   CTD; 1955; -.
DR   GeneTree; ENSGT00940000161177; -.
DR   OMA; YIGPNCN; -.
DR   OrthoDB; 5491831at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00055; EGF_Lam; 5.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF298; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN 9; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00180; EGF_Lam; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..594
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014331250"
FT   TRANSMEM        507..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..247
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          248..294
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          295..342
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          343..393
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          394..445
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          34..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..170
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        220..229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        248..260
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        268..277
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        314..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        326..340
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        368..377
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        419..428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   594 AA;  62354 MW;  4D829285F5B5EE5F CRC64;
     MNGGAERAMR SLRSLGGLAL LCCAAAAAAS AVSPENVTGG GGAAGQVDAS PGPGLRGEPS
     YTFPKATAPT AQARRTGPPR TTVRRPLAAS SSTQSLENTA LRETAGPAST TFQAPLGPSP
     TTPSAVERTS ATPPAPTRPA PTTLSTTTGP APTTPVATTV PAPTTPRTPT PVLPSSSSVL
     PTPPATKGPS PPPPEYVCNC SVVGSLDVNR CNQTTGQCEC QPGYQGLLCE TCKEGFYLNH
     TSGLCLPCDC SPHGALSTLC NSSGKCQCKV GVIGSSCDQC QDGYFGFSKN GCFPCQCNNR
     STSCDALTGA CLNCQENSKG NHCEKCKEGF YQSPDATKEC LRCPCSAVTS TGSCSIKSGK
     LEPECDQCKD GYIGQNCNTC QNGYYNFDSI CRKCQCHGHV DPDKTPKICK PESGECINCL
     HNTTGFWCEN CLEGYAQDLE GNCIKKEVIV PTPEGSTILV SNASLTTSVP SPIINSTFTP
     TTLQTILSTS ENSTSALADV SWTQFNIIIL TVIIIVVVLL MGFVGAVYMY REYQNRKLNA
     PFWTIELKED NISFSSYHDS IPNADVSGLL EDDGNEVAPN GQLTLTTPIH NYKA
//
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