Q86YT9 (JAML1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Junctional adhesion molecule-like

Alternative name(s):
Adhesion molecule interacting with CXADR antigen 1
Dendritic cell-specific protein CREA7-1

Gene names

Name:	AMICA1
Synonyms:	JAML
ORF Names:	UNQ722/PRO1387

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	394 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	May function in transmigration of leukocytes through epithelial and endothelial tissues. Expressed at the plasma membrane of polymorphonuclear leukocytes, it mediates adhesive interactions with CXADR, a protein of the junctional complex of epithelial cells. Enhances myeloid leukemia cell adhesion to endothelial cells. Ref.1 Ref.7
Subunit structure	Interacts with CXADR. Ref.7
Subcellular location	Cell junction. Cell membrane; Single-pass type I membrane protein. Note: Localized at the plasma membrane in areas of cell-cell contacts and at the cell surface of PMN. Ref.1 Ref.7
Tissue specificity	Expression is restricted to the hematopoietic tissues with the exception of liver. Expressed in fetal liver, spleen and thymus. Ref.1
Induction	Up-regulated upon retinoic acid, Me2SO and PMA treatment in differentiating myeloid leukemia cells. Ref.1
Domain	The Ig-like V-type domain 2 mediates interaction with CXADR. Ref.1 Ref.7
Sequence similarities	Belongs to the immunoglobulin superfamily. Contains 2 Ig-like V-type (immunoglobulin-like) domains.
Sequence caution	The sequence BAC03390.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome heterophilic cell-cell adhesion Inferred from direct assay Ref.7. Source: UniProtKB neutrophil chemotaxis Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of immune response Traceable author statement. Source: Reactome transepithelial transport Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW tight junction Inferred from direct assay Ref.7. Source: UniProtKB
Molecular function	cell adhesion molecule binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86YT9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q86YT9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MFCPLKLILLPVLL → MVSG

Note: No experimental confirmation available.

Isoform 3 (identifier: Q86YT9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     258-259: TL → SI
     260-394: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.6
	Chain	20 – 394	375	Junctional adhesion molecule-like		PRO_0000015074
Regions
	Topological domain	20 – 275	256	Extracellular Potential
	Transmembrane	276 – 296	21	Helical; Potential
	Topological domain	297 – 394	98	Cytoplasmic Potential
	Domain	20 – 132	113	Ig-like V-type 1
	Domain	137 – 250	114	Ig-like V-type 2
Amino acid modifications
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	231	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 116		By similarity
	Disulfide bond	155 ↔ 234		By similarity
Natural variations
	Alternative sequence	1 – 14	14	MFCPL…LPVLL → MVSG in isoform 2.		VSP_014830
	Alternative sequence	258 – 259	2	TL → SI in isoform 3.		VSP_014831
	Alternative sequence	260 – 394	135	Missing in isoform 3.		VSP_014832
	Natural variant	94	1	I → N. Ref.2 Ref.4 Corresponds to variant rs17121881 [ dbSNP | Ensembl ].		VAR_049974
	Natural variant	193	1	V → A. Ref.1 Ref.2 Ref.4 Corresponds to variant rs1793174 [ dbSNP | Ensembl ].		VAR_049975
	Natural variant	322	1	I → M. Corresponds to variant rs2298831 [ dbSNP | Ensembl ].		VAR_049976
Experimental info
	Mutagenesis	54	1	K → E: Loss of localization to the plasma membrane. Ref.1
	Sequence conflict	283	1	C → G in AAM15730. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 64B542F9384C7642	FASTA	394	44,339
	10 20 30 40 50 60 MFCPLKLILL PVLLDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS 70 80 90 100 110 120 PGEHAKDEYV LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL 130 140 150 160 170 180 KGESQVFKKA VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE 190 200 210 220 230 240 IVFRYYHKLR MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN 250 260 270 280 290 300 LVFKKTIVLH VSPEEPRTLV TPAALRPLVL GGNQLVIIVG IVCATILLLP VLILIVKKTC 310 320 330 340 350 360 GNKSSVNSTV LVKNTKKTNP EIKEKPCHFE RCEGEKHIYS PIIVREVIEE EEPSEKSEAT 370 380 390 YMTMHPVWPS LRSDRNNSLE KKSGGGMPKT QQAF
	Isoform 2 [UniParc]. Checksum: D7C7F025BB22C026	FASTA	384	43,119
	10 20 30 40 50 60 MVSGDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS PGEHAKDEYV 70 80 90 100 110 120 LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL KGESQVFKKA 130 140 150 160 170 180 VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE IVFRYYHKLR 190 200 210 220 230 240 MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN LVFKKTIVLH 250 260 270 280 290 300 VSPEEPRTLV TPAALRPLVL GGNQLVIIVG IVCATILLLP VLILIVKKTC GNKSSVNSTV 310 320 330 340 350 360 LVKNTKKTNP EIKEKPCHFE RCEGEKHIYS PIIVREVIEE EEPSEKSEAT YMTMHPVWPS 370 380 LRSDRNNSLE KKSGGGMPKT QQAF
	Isoform 3 [UniParc]. Checksum: CD776E7F57AE0CC9	FASTA	259	29,422
	10 20 30 40 50 60 MFCPLKLILL PVLLDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS 70 80 90 100 110 120 PGEHAKDEYV LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL 130 140 150 160 170 180 KGESQVFKKA VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE 190 200 210 220 230 240 IVFRYYHKLR MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN 250 LVFKKTIVLH VSPEEPRSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells." Moog-Lutz C., Cave-Riant F., Guibal F.C., Breau M.A., Di Gioia Y., Couraud P.O., Cayre Y.E., Bourdoulous S., Lutz P.G. Blood 102:3371-3378(2003) [PubMed: 12869515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-54, FUNCTION, VARIANT ALA-193. Tissue: Bone marrow.
[2]	"Dendritic cell specific protein Crea7-1." Ahn J.H., Jung H.R., Lee B.-H., Jeon C.J., Bae Y.-S. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASN-94 AND ALA-193. Tissue: Dendritic cell.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"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] (ISOFORMS 2 AND 3), VARIANTS ASN-94 AND ALA-193. Tissue: Cerebellum and Spleen.
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-34.
[7]	"Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial CAR and a JAM-like protein on neutrophils." Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A., Parkos C.A. Mol. Biol. Cell 16:2694-2703(2005) [PubMed: 15800062] [Abstract] Cited for: INTERACTION WITH CXADR, SUBCELLULAR LOCATION, DOMAIN, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ515553 mRNA. Translation: CAD56620.2. AY093686 mRNA. Translation: AAM15730.1. AY138965 mRNA. Translation: AAN52117.1. AY358362 mRNA. Translation: AAQ88728.1. AK090409 mRNA. Translation: BAC03390.1. Different initiation. AK094399 mRNA. Translation: BAC04347.1. EF444945 Genomic DNA. Translation: ACA05929.1. EF444945 Genomic DNA. Translation: ACA05930.1.
IPI	IPI00183703. IPI00385063. IPI00607549.
RefSeq	NP_001091996.1. NM_001098526.1. NP_694938.2. NM_153206.2.
UniGene	Hs.16291.
3D structure databases
ProteinModelPortal	Q86YT9.
SMR	Q86YT9. Positions 28-251.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86YT9. 4 interactions.
STRING	Q86YT9.
Polymorphism databases
DMDM	71151910.
Proteomic databases
PRIDE	Q86YT9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356289; ENSP00000348635; ENSG00000160593.
GeneID	120425.
KEGG	hsa:120425.
UCSC	uc001psk.2. human.
Organism-specific databases
CTD	120425.
GeneCards	GC11M118064.
H-InvDB	HIX0010176.
HGNC	HGNC:19084. AMICA1.
MIM	609770. gene.
neXtProt	NX_Q86YT9.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14644.
GeneTree	ENSGT00440000034341.
HOVERGEN	HBG055209.
InParanoid	Q86YT9.
OMA	KKTIVLH.
OrthoDB	EOG4B8JD7.
PhylomeDB	Q86YT9.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q86YT9.
Bgee	Q86YT9.
CleanEx	HS_AMICA1.
Genevestigator	Q86YT9.
GermOnline	ENSG00000160593. Homo sapiens.
Family and domain databases
InterPro	IPR007110. Ig-like. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR013106. Ig_V-set. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
Pfam	PF07686. V-set. 2 hits. [Graphical view]
SMART	SM00409. IG. 2 hits. [Graphical view]
PROSITE	PS50835. IG_LIKE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	80588.
SOURCE	Search...

Entry information

Entry name

JAML1_HUMAN

Accession

Primary (citable) accession number: Q86YT9
Secondary accession number(s): B0YIV1 , B0YIV2, Q5DTC6, Q7Z499, Q8N9I7, Q8NF70

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 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.