P14151 (LYAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-selectin

Alternative name(s):
CD62 antigen-like family member L
Leukocyte adhesion molecule 1
Short name=LAM-1
Leukocyte surface antigen Leu-8
Leukocyte-endothelial cell adhesion molecule 1
Short name=LECAM1
Lymph node homing receptor
TQ1
gp90-MEL
CD_antigen=CD62L

Gene names

Name:	SELL
Synonyms:	LNHR, LYAM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. Ref.10
Subunit structure	Interaction with PSGL1/SELPLG and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of PSGL1 and PODXL2, and tyrosine sulfation modifications of PSGL1. Sulfation on Y-51 of PSGL1 is important for L-selectin binding.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in B cell lines and T lymphocytes. Ref.2
Sequence similarities	Belongs to the selectin/LECAM family. Contains 1 C-type lectin domain. Contains 1 EGF-like domain. Contains 2 Sushi (CCP/SCR) domains.
Sequence caution	The sequence CAA34203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAB43536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAB43537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Sushi Transmembrane Transmembrane helix
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome cell adhesion Traceable author statement. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome regulation of immune response Traceable author statement. Source: Reactome
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	glycosphingolipid binding Traceable author statement. Source: BHF-UCL heparin binding Traceable author statement. Source: BHF-UCL protease binding Inferred from physical interaction. Source: BHF-UCL sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Propeptide

29 – 38

10

PRO_0000017475

Chain

39 – 372

334

L-selectin

PRO_0000017476

Regions

Topological domain

39 – 332

294

Extracellular Potential

Transmembrane

333 – 355

23

Helical; Potential

Topological domain

356 – 372

17

Cytoplasmic Potential

Domain

55 – 155

101

C-type lectin

Domain

156 – 192

37

EGF-like

Domain

195 – 256

62

Sushi 1

Domain

257 – 318

62

Sushi 2

Amino acid modifications

Glycosylation

60

1

N-linked (GlcNAc...) Ref.9 Ref.13

Glycosylation

104

1

N-linked (GlcNAc...) Ref.13

Glycosylation

177

1

N-linked (GlcNAc...) Potential

Glycosylation

232

1

N-linked (GlcNAc...) Potential

Glycosylation

246

1

N-linked (GlcNAc...) Potential

Glycosylation

271

1

N-linked (GlcNAc...) Potential

Glycosylation

311

1

N-linked (GlcNAc...) Potential

Disulfide bond

57 ↔ 155

By similarity

Disulfide bond

128 ↔ 147

By similarity

Disulfide bond

160 ↔ 171

By similarity

Disulfide bond

165 ↔ 180

By similarity

Disulfide bond

182 ↔ 191

By similarity

Disulfide bond

197 ↔ 241

By similarity

Disulfide bond

227 ↔ 254

By similarity

Disulfide bond

259 ↔ 303

By similarity

Disulfide bond

289 ↔ 316

By similarity

Natural variations

Natural variant

193

1

F → L. Ref.1 Ref.4 Ref.7
Corresponds to variant rs1131498 [ dbSNP | Ensembl ].

VAR_019134

Natural variant

201

1

E → Q. Ref.7
Corresponds to variant rs2229568 [ dbSNP | Ensembl ].

VAR_019135

Natural variant

213

1

P → S. Ref.3 Ref.7
Corresponds to variant rs2229569 [ dbSNP | Ensembl ].

VAR_019136

Natural variant

369

1

N → D. Ref.7
Corresponds to variant rs4987382 [ dbSNP | Ensembl ].

VAR_019137

Experimental info

Sequence conflict

37

1

D → Y in CAA34203. Ref.4

Sequence conflict

178

1

Y → H in CAA34203. Ref.4

Sequence conflict

214

1

L → F in CAA34203. Ref.4

Sequence conflict

218 – 220

3

SFS → NFN in CAA34275. Ref.2

Sequence conflict

242

1

G → E in CAA34275. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

372

Helix Strand Turn

Details...

Beta strand

40 – 48

9

Helix

50 – 60

11

Beta strand

61 – 64

4

Helix

70 – 79

10

Beta strand

87 – 94

8

Beta strand

97 – 100

4

Turn

101 – 103

3

Turn

109 – 111

3

Helix

122 – 124

3

Beta strand

128 – 131

4

Beta strand

136 – 138

3

Beta strand

142 – 145

4

Beta strand

151 – 157

7

Beta strand

167 – 174

8

Beta strand

177 – 182

6

Beta strand

187 – 191

5

Sequences

	Sequence		Length	Mass (Da)
	P14151 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 6EA9918ECA2D3643	FASTA	372	42,187
	10 20 30 40 50 60 MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW QRARRFCRDN 70 80 90 100 110 120 YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW VGTNKSLTEE AENWGDGEPN 130 140 150 160 170 180 NKKNKEDCVE IYIKRNKDAG KWNDDACHKL KAALCYTASC QPWSCSGHGE CVEIINNYTC 190 200 210 220 230 240 NCDVGYYGPQ CQFVIQCEPL EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT 250 260 270 280 290 300 CGPFGNWSSP EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK 310 320 330 340 350 360 TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK 370 GKKSKRSMND PY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains." Siegelman M.H., Weissman I.L. Proc. Natl. Acad. Sci. U.S.A. 86:5562-5566(1989) [PubMed: 2664786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-193. Tissue: Lymphocyte.
[2]	"Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins." Tedder T.F., Isaacs C.M., Ernst T.J., Demetri G.D., Adler D.A., Disteche C.M. J. Exp. Med. 170:123-133(1989) [PubMed: 2473156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Tonsil.
[3]	"Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor." Camerini D., James S.P., Stamenkovic I., Seed B. Nature 342:78-82(1989) [PubMed: 2509939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-213. Tissue: Lymphocyte.
[4]	"Characterization of a human homologue of the murine peripheral lymph node homing receptor." Bowen B.R., Nguyen T., Lasky L.A. J. Cell Biol. 109:421-427(1989) [PubMed: 2663882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-193. Tissue: Lymphocyte.
[5]	"Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils." Ord D.C., Ernst T.J., Zhou L.J., Rambaldi A., Spertini O., Griffin J., Tedder T.F. J. Biol. Chem. 265:7760-7767(1990) [PubMed: 1692315] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	SeattleSNPs variation discovery resource Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-193; GLN-201; SER-213 AND ASP-369.
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60, MASS SPECTROMETRY. Tissue: Plasma.
[10]	"Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 O-glycans and of tyrosine sulfate residue 51." Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., Michielin O., Schapira M., Spertini O. J. Biol. Chem. 278:37-47(2003) [PubMed: 12403782] [Abstract] Cited for: INTERACTION WITH SELPLG, FUNCTION.
[11]	"Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin." Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D. J. Biol. Chem. 278:26391-26400(2003) [PubMed: 12736247] [Abstract] Cited for: INTERACTION WITH SELPLG.
[12]	"Endoglycan, a member of the CD34 family of sialomucins, is a ligand for the vascular selectins." Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D. J. Immunol. 181:1480-1490(2008) [PubMed: 18606703] [Abstract] Cited for: INTERACTION WITH PODXL2.
[13]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60 AND ASN-104, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"A template for generation and comparison of three-dimensional selectin models." Bajorath J., Aruffo A. Biochem. Biophys. Res. Commun. 216:1018-1023(1995) [PubMed: 7488174] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Functional Glycomics Gateway - Glycan Binding

L-selectin

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25280 mRNA. Translation: AAC63053.1.
X16150 mRNA. Translation: CAA34275.1.
X17519 mRNA. Translation: CAB43536.1. Different initiation.
X17519 mRNA. Translation: CAB43537.1. Different initiation.
X16070 mRNA. Translation: CAA34203.1. Different initiation.
M32414 , M32406, M32407, M32408, M32409, M32410, M32411, M32412, M32413 Genomic DNA. Translation: AAB60700.1.
AK312673 mRNA. Translation: BAG35555.1.
AY233976 Genomic DNA. Translation: AAO48272.1.
AL021940 Genomic DNA. No translation available.

IPI

IPI00218795.

RefSeq

NP_000646.2. NM_000655.4.

UniGene

Hs.728756.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KJB	model	-	A	39-158	[»]
3CFW	X-ray	2.20	A	39-194	[»]

ProteinModelPortal

P14151.

SMR

P14151. Positions 39-350.

ModBase

Search...

Protein-protein interaction databases

STRING

P14151.

PTM databases

GlycoSuiteDB

P14151.

Polymorphism databases

DMDM

126178.

Proteomic databases

PRIDE

P14151.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000236147; ENSP00000236147; ENSG00000188404.

GeneID

6402.

KEGG

hsa:6402.

UCSC

uc001ggk.1. human.

Organism-specific databases

CTD

6402.

GeneCards

GC01M169659.

H-InvDB

HIX0199982.

HGNC

HGNC:10720. SELL.

HPA

CAB002144.

MIM

153240. gene.

neXtProt

NX_P14151.

Orphanet

34145. Berger disease.

PharmGKB

PA35642.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05451.

HOVERGEN

HBG052375.

InParanoid

P14151.

OrthoDB

EOG4FFD22.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P14151.

Bgee

P14151.

CleanEx

HS_SELL.

Genevestigator

P14151.

GermOnline

ENSG00000188404. Homo sapiens.

Family and domain databases

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR016060. Complement_control_module.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR016348. L-selectin.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
G3DSA:2.10.70.10. Complement_control_module. 2 hits.

KO

K06495.

PANTHER

PTHR19325:SF20. PTHR19325:SF20. 1 hit.

Pfam

PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]

PIRSF

PIRSF002421. L-selectin. 1 hit.

PRINTS

PR00343. SELECTIN.

SMART

SM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.
SSF57535. Complement_control_module. 2 hits.

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24874.

PMAP-CutDB

P14151.

SOURCE

Search...

Entry information

Entry name

LYAM1_HUMAN

Accession

Primary (citable) accession number: P14151
Secondary accession number(s): B2R6Q8, P15023

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.