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Database: UniProt
Entry: A0A3B4U873_SERDU
LinkDB: A0A3B4U873_SERDU
Original site: A0A3B4U873_SERDU 
ID   A0A3B4U873_SERDU        Unreviewed;       681 AA.
AC   A0A3B4U873;
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=Stromal interaction molecule 1-like {ECO:0000313|Ensembl:ENSSDUP00000014836.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000014836.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000014836.1}
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}.
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DR   AlphaFoldDB; A0A3B4U873; -.
DR   STRING; 41447.ENSSDUP00000014836; -.
DR   Ensembl; ENSSDUT00000015120.1; ENSSDUP00000014836.1; ENSSDUG00000010826.1.
DR   GeneTree; ENSGT00390000000214; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0051049; P:regulation of transport; IEA:UniProt.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   CDD; cd11722; SOAR; 1.
DR   Gene3D; 1.10.238.180; -; 1.
DR   Gene3D; 1.10.287.3550; -; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR032393; SOAR.
DR   InterPro; IPR037608; STIM.
DR   PANTHER; PTHR15136:SF9; STROMAL INTERACTION MOLECULE 1; 1.
DR   PANTHER; PTHR15136; STROMAL INTERACTION MOLECULE HOMOLOG; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF16533; SOAR; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..681
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017436329"
FT   TRANSMEM        208..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..181
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          561..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          245..335
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        600..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  76865 MW;  2B949051AE9A1A90 CRC64;
     MEFNKFVTLW IFCLCLVGES WTDKTSSPTS DSQIVENEVS DFCRIDEPLC NDENARLSFE
     AIGSIHNQMD DDANGNVDVV ETDGFLREDL NYHDPKAKHN SFHGDDQFIS VEDLWNAWKS
     SEVYNWTVDE VVEWLITYVE LPQYVDAFRK MNFNGSAMPR LAVKNTTLTL SILKILDRSH
     VQKLQLKSLD TVLFGAPLMN RHNHLKDFML VVSIVIGMGG CWFAYIQNRY SKDHMKKMMK
     DLEGLQRAEQ SLHDLQQKLQ IAQEEHRTVE VEKVNLEQKL RDEINAAKQE AQRLRELREG
     TENELSRQKY AEEELEQHKG EALKVRMALK KAEKELESRS SWSPPESLQK WLQLTHEVEV
     QYYNIKKQNA ERQLLVAKEG AEKIKKKRNT LFGTFHVAHS SSLDDVDHKI LAAKQALGEV
     TAALRERLHR WQQIEILTGF TIVNNPGLPS LASSLNLDPS FMGGRATPQH FIMSDDMDDL
     DEDIMPGTLQ SPSMMSLRQR HIDPQLAMGS QRDLNRSDSD SSLSLSQVGD RLSAYSSKGH
     LMKPASLMHG LSSRTEDAIS LHAHTPNGGN RIHEGSPAEL VPDSPILMKK VYGMEKSPSL
     GEINSLSESS RSLSPNSTEP DTPSPTGGQL GVVGPKGSTR IPQLSSKKSP LEEDSGSTGE
     DTDSTASRKK HTFKIFKKQK K
//
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