ID A0A498LDR0_LABRO Unreviewed; 1536 AA.
AC A0A498LDR0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=p-selectin {ECO:0000256|ARBA:ARBA00044174};
DE AltName: Full=CD62 antigen-like family member P {ECO:0000256|ARBA:ARBA00044221};
DE AltName: Full=Granule membrane protein 140 {ECO:0000256|ARBA:ARBA00044337};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 3 {ECO:0000256|ARBA:ARBA00044355};
DE AltName: Full=Platelet activation dependent granule-external membrane protein {ECO:0000256|ARBA:ARBA00044292};
GN ORFNames=ROHU_032902 {ECO:0000313|EMBL:RXN06302.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN06302.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN06302.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN06302.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN06302.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and PODXL2
CC and mediates neutrophil adhesion and leukocyte rolling. This
CC interaction requires the sialyl-Lewis X epitope of SELPLG and PODXL2,
CC and specific tyrosine sulfation on SELPLG.
CC {ECO:0000256|ARBA:ARBA00044001}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family.
CC {ECO:0000256|ARBA:ARBA00007360}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN06302.1}.
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DR EMBL; QBIY01013374; RXN06302.1; -; Genomic_DNA.
DR STRING; 84645.A0A498LDR0; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 15.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 16.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR033991; Selectin_CTLD.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR19325:SF484; P-SELECTIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 3.
DR Pfam; PF00084; Sushi; 16.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 16.
DR SMART; SM00034; CLECT; 3.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 16.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 3.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50923; SUSHI; 16.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000313|EMBL:RXN06302.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 28..148
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 148..185
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 188..251
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 252..315
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 316..379
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 380..443
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 444..507
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 508..571
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 572..635
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 636..699
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 700..763
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 764..825
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 874..995
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 997..1118
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1118..1154
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1157..1218
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1233..1281
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1282..1343
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1344..1405
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1406..1467
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1468..1535
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 175..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 222..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 350..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 478..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 606..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 734..761
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1144..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1189..1216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1252..1279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1314..1341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1376..1403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1438..1465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1506..1533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1536 AA; 172027 MW; FDC4E2E98EAB54DA CRC64;
MGIFNKVPLQ FFASLVLIYS VLNIWRGTAG WSYHYSESRM DWESARRWCR EKFTDMVAIQ
NKEEIYHLNR ILPKVAGYYW IGIRKISGRW TWVGTNKLLT NEAENWAEKE PNNGGNNEDC
VEIYIKREKD EGKWNDESCL KQKTALCYTA ACKDDSCVSG HGECVETINS HKCSCFEGFY
GERCEHVVKC KPEHVSPPDH ASVQCSDPNG NSSYASQCEY SCEKGYELKG SRTTRCTSTT
KWSSKPPTCE LFQCPELTKP QKGQMQCQHP MGSFSYQSTC EFMCEEGYTM RDSSSSTLFC
GATGHWNDSQ PTCEIVKCKP EDVTQPDHAI VRCSHPSENF SYGSQCEYSC EEGYEVKGSR
TTTCTSTTEW SKKPPTCEPV QCPELTKPQK GQMQCQHPMG SFSYQSTCEF VCEEGYTVQD
SSSSTLFCEA MGHWNDSQPT CEIIKCKPED VSPPDHASVQ CSDPNGNFSY GSQCEYSCEE
GYELKGSRTT TCTSTTEWSS KPPTCELVQC PELTKPQKGQ MQCQDQMGIF SYQSTCEFIC
EEGYKVQDSS SSTLFCEATG RWNDSQPTCE IIKCKPEDVS PPDHASVQCF DPNGNSSYAS
QCEYSCEKGY ELQGSRTTTC TSTTEWSSKP PTCELVQCPE LTKPQKGQMQ CQHPMGSFSY
QSTCEFVCEE GYTVQDSSSS TLFCGATGHW NDSQPTCEII KCKPEDVSPP DHASVQCSHP
SENFSYGSQC EYSCKEGYEL KGSRTTTCTS TTEWSSKPPT CEPVVCPQLP EPINSYMNCS
SEEPTVGTFC TFSCHEGHQL EDLSNRIVIC NYNGSWSGEV AVCQAHPDTS TSLLEATEVT
IGVSSAMSAS SLGLVLWLLK RMRRKADNFD LNSVEGWTYH FLDNETMTWN HTRTYCQKHY
TDIVMVYDEN VTRFLQEKLT KKSSSPYYWI GMQKINGNWT WVANGQTANY ENWADNEPNN
NLSNENCVEL YISKGNNSGK WNDESCEYKK HPVCQTVKAW TYHYKTDINM DWTTARQWCQ
KNYTDMVAIQ NQEEVEYLNQ VLPFSQAYYW IGIRKIDGYW TWVGTNKRLD SEAANWAKDE
PNNKGSGQDC VEIYIKRSRE TAKWNDERCS KKKATVCYLA SCSKKSCSEH AECVETIGNY
RCQCHPGFKG PRCEEVVQCW PIGNPQQGFV KCDGVFGGFH FNSSCQFQCA TGFKLEGAQR
LHCLASGHWD NALPVCQAVQ CLPIIDTPGG WRMNCTHPLS INSYDSSCDF ECEDGFELKG
SKTTLCDQTG QWTHKPPTCT VVTCNAILAP ANGHLTCADP LGKFSFNSSC NVSCDEGYKL
RGKATLTCLS AGNWSAPTPV CEVVKCDPLR PIPHGFLQCH DPVEEFAYGS TCWLKCDTGF
VHTGKNFTHC TKQGNWSHIP PVCQVIRCGA LESVQHGSVH CQDPLGEFSY GSLCWLECVA
GFTLNGSNST YCTSQGKWSQ EFPVCQAVRC EPLSLSHPPE LGLSPSMNCS HPHGNFSFGS
QCIFRCAESH KLNGTSQLIC TSSGYWTNSP PSCAVG
//
