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Database: UniProt
Entry: A0A3B5QGF0_XIPMA
LinkDB: A0A3B5QGF0_XIPMA
Original site: A0A3B5QGF0_XIPMA 
ID   A0A3B5QGF0_XIPMA        Unreviewed;       970 AA.
AC   A0A3B5QGF0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Protein phosphatase 1 regulatory subunit 29-like {ECO:0000313|Ensembl:ENSXMAP00000030619.1};
GN   Name=ELFN2 {ECO:0000313|Ensembl:ENSXMAP00000030619.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000030619.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000030619.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030619.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_005809662.1; XM_005809605.1.
DR   AlphaFoldDB; A0A3B5QGF0; -.
DR   STRING; 8083.ENSXMAP00000030619; -.
DR   Ensembl; ENSXMAT00000033829.1; ENSXMAP00000030619.1; ENSXMAG00000009997.2.
DR   GeneID; 102225909; -.
DR   KEGG; xma:102225909; -.
DR   GeneTree; ENSGT00940000159737; -.
DR   InParanoid; A0A3B5QGF0; -.
DR   OMA; KNRCGAP; -.
DR   OrthoDB; 4176548at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR24369:SF204; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 29-RELATED; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 2.
PE   4: Predicted;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..970
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017457023"
FT   TRANSMEM        404..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..244
FT                   /note="LRRCT"
FT                   /evidence="ECO:0000259|SMART:SM00082"
FT   REGION          469..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..676
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   970 AA;  105020 MW;  B44EF13866250A2E CRC64;
     MAARQLLSFP SPSLLLPVLL AALLLLRLPA AVKGDCWLIE GDKGYVWLAI CSQNQPPYET
     IPQHINSTVH DLRLNENKLK AVLFTSMYRF TNLTDLNLTK NEISYIEDGA FAGQANLQVL
     QLGYNKLTNL TEGMLRGLGR MQCLFLQHNL IEVIATNAFW ECPNLSSLDL SSNKLARLDP
     STFTSLNRLM VCELAANPFH CGCELYSFLT WLEEFNNVTH TYDRLQCETP PELTGYPLLG
     QAPGQGRNAR NILLSACRDG VIIPGMTSQM PDPDGSGMGL DNSDPGLYPQ PTTATADPNY
     VPQISIKLES VSLYTASLLV QIPKPYTKMY ILSQYNDTFA TEIMSLTKKK EKIPIDKLKP
     HTNYTYCVAS GSKTQRYNHT CLSFTTRAMG PEDLRSNPST TTHYIMTILG CLFGMVIVLG
     FVYYCLRRRR IQEEKEKAIS VKKTILEMRY GPEAAAAVAN DPGAIQRLQE QTHHHHSGGA
     GGKLPPSASS STGMLHGSAN TSSSRLSTLP QVEKMASAFS EAMGSKSNYM DVRTTGMVGE
     SRDGVLVAGG VGGEVLVDMR GVAENGTEAG EDSDDDGRGS ASEISTIAKE VDKVNQIINN
     CIDALKLDAS ANIVSTADDG NSLSSSQPPC MAPLSRNLLP LSTASSGDQI MASSPKVHPK
     SQPHPQPHPQ PQPQSHPQSH PQLHQQPHPP SMAPVPLVMP LSERPGISGG GFLSPPYRDP
     PPANAVRPLQ RQQSADTAVV KNRCGTPAAV SVKNTRLYSV DIPEQRSDPP KYPTEKGSPA
     VCGGMGGSGG HGGVGGCGGN GKGNLNGGGV SLNGGGMGCN NGNGSGCGVA GPGQQQHHLE
     VQPDYHSSEH RHSFPALYYE DGNESPLPAQ KASFLKPLGR TKREATATYS QLSPSRHHNY
     NSGYSSSPEY SSESTLRIWE RFRPYKKNPR EEASYIAAGH ALRKKVQFAK DEDLHDILDY
     WKGVSAQQKL
//
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