ID U3JR69_FICAL Unreviewed; 318 AA.
AC U3JR69;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Transmembrane protein with EGF like and two follistatin like domains 1 {ECO:0008006|Google:ProtNLM};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000005273.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000005273.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000005273.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the tomoregulin family.
CC {ECO:0000256|ARBA:ARBA00038484}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; U3JR69; -.
DR Ensembl; ENSFALT00000005299.2; ENSFALP00000005273.2; ENSFALG00000005068.2.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000160714; -.
DR HOGENOM; CLU_048579_1_0_1; -.
DR Proteomes; UP000016665; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00104; KAZAL_FS; 2.
DR Gene3D; 3.30.60.30; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR PANTHER; PTHR21632:SF3; TOMOREGULIN-1; 1.
DR PANTHER; PTHR21632; UNCHARACTERIZED; 1.
DR Pfam; PF07648; Kazal_2; 2.
DR SMART; SM00280; KAZAL; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51465; KAZAL_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..83
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 127..175
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 209..249
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 297..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 239..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 318 AA; 35259 MW; E8EC25F941617ABD CRC64;
MLRGLRTRES DVRVCDESSC KYGGVCKEEG DGLKCACQFQ CHTNYIPVCG SNGDTYQNEC
FLRRAACKHQ KEITMVSRGP CYSDNGSGSG EGEYEGSGTE VQRKHSKCGV CKYRAECDED
AENVGCVCNI DCSGYSFNPV CASDGSSYNN PCFVREASCL RQEQIDIRHL GHCSETDDTN
AVGKKDDGMQ YRPEVKDASD QREDIYIGNH IPCSESFNGY CIHGKCEFIY STQKASCRCE
SGYTGQHCEK TDFSILYVVP SRQKLTHVLI AAIIGAVQIA IIVAIVMCIT RKCPKNNRGR
RQKQNLGHFT SDTSSRMV
//
