SUREJ_STRPU
ID SUREJ_STRPU Reviewed; 1450 AA.
AC Q26627;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Sperm receptor for egg jelly;
DE Short=suREJ;
DE Flags: Precursor;
GN Name=REJ;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS ALA-440;
RP PRO-593; MET-1204; SER-1371; ALA-1390 AND VAL-1443.
RC TISSUE=Testis;
RX PubMed=8666666; DOI=10.1083/jcb.133.4.809;
RA Moy G.W., Mendoza L.M., Schulz J.R., Swanson W.J., Glabe C.G.,
RA Vacquier V.D.;
RT "The sea urchin sperm receptor for egg jelly is a modular protein with
RT extensive homology to the human polycystic kidney disease protein, PKD1.";
RL J. Cell Biol. 133:809-817(1996).
CC -!- FUNCTION: Receptor for the egg jelly ligands inducing the acrosome
CC reaction. Could be a regulator of sperm ion channels.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Present on the surface of the sperm flagellum and also on
CC a thin belt of membrane directly over the acrosomal granule at the
CC anterior apex of the sperm head.
CC -!- DEVELOPMENTAL STAGE: Expressed at the earliest stage of spermiogenesis.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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DR EMBL; U40832; AAB08448.1; -; mRNA.
DR PIR; T30273; T30273.
DR RefSeq; NP_999773.1; NM_214608.1.
DR AlphaFoldDB; Q26627; -.
DR SMR; Q26627; -.
DR TCDB; 1.A.5.1.4; the polycystin cation channel (pcc) family.
DR EnsemblMetazoa; NM_214608; NP_999773; GeneID_373460.
DR GeneID; 373460; -.
DR KEGG; spu:373460; -.
DR CTD; 373460; -.
DR eggNOG; KOG3599; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_265129_0_0_1; -.
DR InParanoid; Q26627; -.
DR OMA; FDIHIST; -.
DR OrthoDB; 1276906at2759; -.
DR PhylomeDB; Q26627; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 3.10.100.10; -; 2.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR014010; REJ_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00059; Lectin_C; 2.
DR Pfam; PF02010; REJ; 1.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51111; REJ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1450
FT /note="Sperm receptor for egg jelly"
FT /id="PRO_0000024301"
FT TOPO_DOM 27..1414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1415..1435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1436..1450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..63
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 77..190
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 210..324
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 468..1187
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1353..1403
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 36..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 53..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 98..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 165..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 231..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 297..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 440
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:8666666"
FT VARIANT 593
FT /note="A -> P"
FT /evidence="ECO:0000269|PubMed:8666666"
FT VARIANT 1204
FT /note="I -> M"
FT /evidence="ECO:0000269|PubMed:8666666"
FT VARIANT 1371
FT /note="C -> S"
FT /evidence="ECO:0000269|PubMed:8666666"
FT VARIANT 1390
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:8666666"
FT VARIANT 1443
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:8666666"
SQ SEQUENCE 1450 AA; 158165 MW; 66C322FB26F918F5 CRC64;
MSVFVILILF NAILNFKTVG PAAVSSKTVD CASAPCMNGG TCADGFNNFT CFCEEGFTGS
MCETEYGCFR PWFYGPAFGY CYLWERVDYN WTQARESCID QGRGAELASI HSAEENAFVY
AQIRRYAWIG LSDQVTEGVF DYADGTPVDY LSFPDKNKQS ETRDCVYVKH LRVDNWSLLD
CRANKTSICK STTTFSATDG CATGWVHNPA TGYCYFYEER GGMWSKGREF CLDAGADLAS
IHSAEENAFI FDMLTEFVWL GLNDLETEGV YTNFSDGTPA DFDNFPADNY QNEDHDCVSI
RHLEKTDRYW FFLGCDDTVT SICKRPHEVV ATQAPPYLFT TTDVPATTTT IPTTTTTISA
TTRTIDAMIL IELLLFPNNV SSIDNIFRVN NTILVTASVL GSFQALSSQI LWSITNHLSG
DSVQYTVYSE DAVLVRFTTV SIFTIKATAV GNSHNLTATA NATVKHVCIS SLTTSVKEHC
DAPHPAVYLR AFDIHISTHM ELNGKCIDPM TPDFKWRIFT STEADDVVTA FEKITHTRQV
MIPRGTLPYG IYSLNLNAKT RLKTSGEVTG EKEIISWLEI QPPPLVAVIK GGASRSHGVS
SNLIVDGSNS YDPDVPPGSS SNVTFLWYCV VVDPDVMYSS LDEAIQNTDN ACFEDEGIMM
NSTSSMIEVI ANKLNANVTM NFWLNISKEG QISGLTQQRI HLTLGLLPEI EISCISNCNM
YIFTAERLVL HASCTNCDSE NEDVSFRWSL ESNHTSVIGD LSSQTTTGLD QPYLVLKPLT
FDSISEMGSI ILRVTGSQSD SDGYAEFSVD LPHNAPPALG SCVVTPDEGY ALQTDFTVTC
SNFTDVDEPL TYQIILFSHV DVVDWMFVGR GEGFQLYEGS APIKDGLYLP VGVGTDDHDI
LLQVNVRDCN MASTSVYISA TVHPPTLDAV GMNLVQELLD MALLVETNVN ALLAVGDPGQ
AAQLISALGS ILNSIGDEDD SEEGRETRSE IRSFLVDCVA AIPVESMTSL KQSSAALAVV
THNKQEISTH VQMLAASTLS EMTSFVKSKS GSYTQAQENI ESAGTILVEG LSNILSAAKE
TERLLSDDTS QEREDHKNLI EVAVSTINDI QDAIVAGKIP SEAATIITSP ALSIAVGSIS
RDELAEATFG GPEDLGSFRM PSQDVLNQAM EHALGTTVSM KMSAMKWNPF SWPGAGGESI
KSSIVGIQLE ADQMLEFHDL TADIDVYLPM RETLSADPVS VHITKTSSDS VLIDHSSLPV
DGALHLTVIA ENEPMVALSI CTARISITES SCVGTDTPLG VSNEDPDTDA NFTWTVPLVD
LKAADGIMIR LYDSEDQPGY ENDNITLSVF MHTLQCNFWN EDQQEWDSTG CKVGPLSKPS
TTHCLCNHLT GFFGSSILVP PNHAQPVIGG HKLTGVDFLI CVLIGYGIYC VALVIRVVGC
SFAIRVHKVL
