ID   SP15_TETCF              Reviewed;         697 AA.
AC   P19965;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=SITS-binding protein;
DE   AltName: Full=SP105;
OS   Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2775201; DOI=10.1042/bj2610155;
RA   Jentsch T.J., Garcia A.M., Lodish H.F.;
RT   "Primary structure of a novel 4-acetamido-4'-isothiocyanostilbene-2,2'-
RT   disulphonic acid (SITS)-binding membrane protein highly expressed in
RT   Torpedo californica electroplax.";
RL   Biochem. J. 261:155-166(1989).
CC   -!- FUNCTION: This glycoprotein is probably not a functional part of the
CC       chloride channel.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Electroplax tissue, brain (200-fold less), and
CC       heart (500-fold less).
CC   -!- MISCELLANEOUS: Binds 4-acetamido-4'-isothiocyanostilbene-2,2'-dis
CC       ulphonic acid (SITS), an inhibitor of a variety of anion transport
CC       proteins.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC   -!- CAUTION: Although related to the glycosyl hydrolase 31 family, lacks
CC       the conserved active sites, suggesting it has no glycosidase activity.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X16078; CAA34209.1; -; mRNA.
DR   PIR; S04987; S04987.
DR   AlphaFoldDB; P19965; -.
DR   SMR; P19965; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..697
FT                   /note="SITS-binding protein"
FT                   /id="PRO_0000072054"
FT   TOPO_DOM        2..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   697 AA;  78457 MW;  985DEEC41EC6E2F5 CRC64;
     MARRAKKMAS NSGDSSPEPG IKEINETWKG AIACLGVALL FLMTIGVLYW QVVEKPDTNW
     VLRGQVSGLV WDKKSLSFSF KSLSQDKTFA RIDARHLPVR GGALLNNHCW FNTTRFCHTW
     DGVANLQVTL DTPNQSVAEC YRVEWTPLNC QVALQDCFSM VNTSWYGGGS MRLQYWPINN
     ANINSQPFVI SDLQDTPTGY GSVLERYFLG STGVAVRVHQ EVPLHVGIES RKQLCLGIPP
     NAEMQPLRYT ICVSDSLRSA HQQFGTVIPV VQPDQPDTSI LRLPHWRSQR VADIALKLEH
     NLKTFTRKLK LHRLGEGIMD LGEQSTLLLS NEVDETLQSQ NRYRGLRQLR LSITLSPFTS
     IDSHHFQTTL QEGRENLWLG LPSAANGSQG PLLMKWKGKF AVKLNISNEE AQDWFIEQVH
     SLQRRLEVDY VNLEVGVGSP YVGQAQHHSC RLCGDDYINQ FALLAEKLGN GTTVSAATRT
     AHLPVFVRMV PRQSDWSHAG LKGLIPSILH YSLLGYSFFI PDVIGGSLTD GFLADEELFV
     RWMQIATFLP VMSFSTPPWV FGETWIVNVT RSCIHRHQTF VVPLLMKYAA EWTSLGHPVF
     RPLWWVSPSD PNTFTINDEF LIGDEVLVAP VTESGKVHRD IYLPGNSFQW KDMNTAQVFE
     GGTLLREYPV ALTEVAVFIR QKSKYTPAIA EIQQATT