ID A0A0A0B006_CHAVO Unreviewed; 527 AA.
AC A0A0A0B006;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
DE Flags: Fragment;
GN ORFNames=N301_09619 {ECO:0000313|EMBL:KGL99502.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL99502.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL99502.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL99502.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KL873593; KGL99502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0B006; -.
DR STRING; 50402.A0A0A0B006; -.
DR Proteomes; UP000053858; 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:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 6.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 6.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
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; 1.
DR Pfam; PF00084; Sushi; 6.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 6.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 6.
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:KGL99502.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 1..119
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 119..155
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 158..219
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 220..281
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 282..343
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 344..405
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 406..467
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 468..527
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 145..154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 190..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 252..279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 314..341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 376..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 438..465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 500..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL99502.1"
FT NON_TER 527
FT /evidence="ECO:0000313|EMBL:KGL99502.1"
SQ SEQUENCE 527 AA; 57276 MW; C16B1B2BBB968107 CRC64;
WTYHYSDQGD YTWEQARNYC QTFFTDLVAI QNKHEIEYLN KSLPFHGRYY WIGIRKLGGT
WTWVGTRKAL TKEAENWAAG EPNNRRSNQD CVEIYIKRQQ ESGKWNDEPC SRKKKALCYR
ASCQPFPCSQ RGECVETIGS YRCECYPGFH GPECEDAITC PVLNPPDRGE LNCSHLHGDF
AFGSKCAFSC QMGFALTGPE SRECMATGTW TGDAPRCEAI TCPVLSAPDQ GQLNCSHPHG
DFAFGSTCVF SCQMGFALMG PESRECMATG TWTGDAPRCE AIVCPVLSAP DRGGLNCSHL
HGDFTFGSTC AFSCQTGFAL MGSKSRECTA TGTWTGDEPR CEAITCPVLS APDRGKLNCS
HPHGDFAFGS TCAFSCQMGV ALTGPDSHEC TATGIWTGDV PQCKVIKCSA LAVPKMGQAA
CSHLHGDFTF GSTCAFSCQA GFVLMGLENL KCTATGTWTG DTPQCKAISC PVLDAPSSGQ
LSCSHMHGNF TYNSTCTFSC EEGFVRMGAE VLRCAATGNW TRHPPVC
//
