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Database: UniProt
Entry: W5MFC4_LEPOC
LinkDB: W5MFC4_LEPOC
Original site: W5MFC4_LEPOC 
ID   W5MFC4_LEPOC            Unreviewed;      1061 AA.
AC   W5MFC4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Si:ch73-215d9.1 {ECO:0000313|Ensembl:ENSLOCP00000007083.1};
GN   Name=KIAA0319 {ECO:0000313|Ensembl:ENSLOCP00000007083.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007083.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000007083.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AHAT01017928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01017929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01017930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MFC4; -.
DR   Ensembl; ENSLOCT00000007091.1; ENSLOCP00000007083.1; ENSLOCG00000005830.1.
DR   GeneTree; ENSGT00940000161462; -.
DR   Proteomes; UP000018468; Linkage group LG11.
DR   Bgee; ENSLOCG00000005830; Expressed in brain and 3 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   CDD; cd00146; PKD; 4.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029865; KIAA0319-like.
DR   InterPro; IPR013980; MANSC_dom.
DR   InterPro; IPR011106; MANSC_N.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR46182:SF1; DYSLEXIA-ASSOCIATED PROTEIN KIAA0319; 1.
DR   PANTHER; PTHR46182; FI19480P1; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00765; MANEC; 1.
DR   SMART; SM00089; PKD; 5.
DR   SUPFAM; SSF49299; PKD domain; 4.
DR   PROSITE; PS50986; MANSC; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        945..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..87
FT                   /note="MANSC"
FT                   /evidence="ECO:0000259|PROSITE:PS50986"
FT   DOMAIN          537..609
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          199..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  116327 MW;  EFEF4710853BBFC8 CRC64;
     LFLCTTGAFA DPCWQGVTFS ETIISPNLKN TNILRVPDVV SLTQCAGACC DFPGCDLAWL
     FERHCYIVNC KHKENCEPKK RPGTDSYMIF LQRRPPQTLV LQSLVRGQPF SGRVRPQSNL
     KGPESLKDLA LFDGDQAFED SSLAEDEYPE SYRSSIIHGS PVGSRAEQKE SSGYLDWLSV
     AGKEGFNFSE YGVSQGDLYT SQSPSKSSLL QRSTSTKGEI DRGDAPTVPA PATPVSLSGQ
     LLVASLLKLQ SLYGTPAILD DVPLHNISLT SMEMMPTSHN STADFISEIQ IQPSLPDVPS
     SPPTSTSSPT TTLTPGTAEG TSVKALVVSA GDNVEVTLPR NTVELNAFVF PEPKTEVSYS
     YEWSLISHPA DYEGEMENKH TKTLKLSRLS PGLYIFKVCV TAGSSYGEGF VNITVKAATQ
     VNQPPVAIAS PWIQEISLPT TSTYIDGSQS TDDDKIVSYH WEEVTGPLRE QKASADTAIL
     HLYDLVPGNY TFRLTVIDSD GAANSTTATV LVHKPTDYPP VANAGPNQAI TLPHNYITLS
     GNQSSDDHGI VSYEWSLSPA SKGKVVAIQG VRTPYLQLSA MQEGDYTFQL TVTDSAGQQA
     TAMVTVIVQP ENNSPPQAVV GPDKELTFPA ESTTLDGSRS TDDQGVVSFL WDCISGPSGA
     KIEKADKPLA IVTGLRIGTY KFRLTVKDQQ GLTSDGIITV TLKEEKNAPP VARAGGSHVL
     VLPNNSVILD GSASTDDQGI VSYRWVRDGQ SPASGDVIYG SEHQAVLHLT NLVEGTYIFQ
     LHVTDAKGYS STDAATVEVC PDPHRKDEVE LELYVGVSQL NQQQKDTVVR QLAVLLNVLD
     SDIIVQKVQA QTELSTVMSF YVRGREGILQ GPQLTRTLRG QLLKEKSDFL LFRVLRVDTA
     VCLLRCSEHG QCDPITKHCV CDPFWVENPV HRYFNDGESN CEWSVLYVII TSFVMVILIM
     GLSWACVCCC KRTRRTKVRK KTKYTILDNI DEQERMVLRP KYNIKHRSTE HNSSLMISES
     EFESEQDTIF TREKVDKEKM KNSSNGSAQN GDVFSFHPED R
//
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